EC |
1.1.3.17 |
Accepted name: |
choline oxidase |
Reaction: |
choline + 2 O2 + H2O = betaine + 2 H2O2 (overall reaction) (1a) choline + O2 = betaine aldehyde + H2O2 (1b) betaine aldehyde + O2 + H2O = betaine + H2O2 |
Glossary: |
choline = (2-hydroxyethyl)trimethylammonium
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Systematic name: |
choline:oxygen 1-oxidoreductase |
Comments: |
A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-67-5 |
References: |
1. |
Ikuta, S., Imamura, S., Misaki, H. and Horiuti, Y. Purification and characterization of choline oxidase from Arthrobacter globiformis. J. Biochem. (Tokyo) 82 (1977) 1741–1749. [PMID: 599154] |
2. |
Rozwadowski, K.L., Khachatourians, G.G. and Selvaraj, G. Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli. J. Bacteriol. 173 (1991) 472–478. [DOI] [PMID: 1987142] |
3. |
Rand, T., Halkier, T. and Hansen, O.C. Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis. Biochemistry 42 (2003) 7188–7194. [DOI] [PMID: 12795615] |
4. |
Gadda, G., Powell, N.L. and Menon, P. The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Arch. Biochem. Biophys. 430 (2004) 264–273. [DOI] [PMID: 15369826] |
5. |
Fan, F. and Gadda, G. On the catalytic mechanism of choline oxidase. J. Am. Chem. Soc. 127 (2005) 2067–2074. [DOI] [PMID: 15713082] |
6. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
7. |
Fan, F., Ghanem, M. and Gadda, G. Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance. Arch. Biochem. Biophys. 421 (2004) 149–158. [DOI] [PMID: 14678796] |
8. |
Gadda, G. Kinetic mechanism of choline oxidase from Arthrobacter globiformis. Biochim. Biophys. Acta 1646 (2003) 112–118. [DOI] [PMID: 12637017] |
|
[EC 1.1.3.17 created 1978, modified 2005, modified 2007] |
|
|
|
|
EC |
1.1.99.1 |
Accepted name: |
choline dehydrogenase |
Reaction: |
choline + acceptor = betaine aldehyde + reduced acceptor |
Glossary: |
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium |
Other name(s): |
choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase; choline:(acceptor) 1-oxidoreductase |
Systematic name: |
choline:acceptor 1-oxidoreductase |
Comments: |
A quinoprotein. In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-67-5 |
References: |
1. |
Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O. Mammalian choline dehydrogenase is a quinoprotein. Agric. Biol. Chem. 49 (1985) 3623–3626. |
2. |
Ebisuzaki, K. and Williams, J.N. Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria. Biochem. J. 60 (1955) 644–646. [PMID: 13249959] |
3. |
Gadda, G. and McAllister-Wilkins, E.E. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl. Environ. Microbiol. 69 (2003) 2126–2132. [DOI] [PMID: 12676692] |
4. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
|
[EC 1.1.99.1 created 1961, modified 1989, modified 2005] |
|
|
|
|
EC |
1.2.1.8 |
Accepted name: |
betaine-aldehyde dehydrogenase |
Reaction: |
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+ |
Glossary: |
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium |
Other name(s): |
betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB |
Systematic name: |
betaine-aldehyde:NAD+ oxidoreductase |
Comments: |
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-90-4 |
References: |
1. |
Rothschild, H.A. and Barron, E.S.G. The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase. J. Biol. Chem. 209 (1954) 511–523. [PMID: 13192104] |
2. |
Livingstone, J.R., Maruo, T., Yoshida, I., Tarui, Y., Hirooka, K., Yamamoto, Y., Tsutui, N. and Hirasawa, E. Purification and properties of betaine aldehyde dehydrogenase from Avena sativa. J. Plant Res. 116 (2003) 133–140. [DOI] [PMID: 12736784] |
3. |
Muñoz-Clares, R.A., González-Segura, L., Mújica-Jiménez, C. and Contreras-Diaz, L. Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol. Chem. Biol. Interact. (2003) 129–137. [DOI] [PMID: 12604197] |
4. |
Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jornvall, H. and Eklund, H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7 (1998) 2106–2117. [DOI] [PMID: 9792097] |
5. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
|
[EC 1.2.1.8 created 1961, modified 2005, modified 2011] |
|
|
|
|
EC |
1.2.1.73 |
Accepted name: |
sulfoacetaldehyde dehydrogenase |
Reaction: |
2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+ |
Glossary: |
2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate |
Other name(s): |
SafD |
Systematic name: |
2-sulfoacetaldehyde:NAD+ oxidoreductase |
Comments: |
This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A.M. and Smits, T.H.M. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190 (2008) 159–168. [DOI] [PMID: 18506422] |
|
[EC 1.2.1.73 created 2008] |
|
|
|
|
EC |
1.3.8.13 |
Accepted name: |
crotonobetainyl-CoA reductase |
Reaction: |
γ-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein |
Glossary: |
γ-butyrobetainyl-CoA = 4-(trimethylammonio)butanoyl-CoA
crotonobetainyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA |
Other name(s): |
caiA (gene name) |
Systematic name: |
γ-butyrobetainyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase |
Comments: |
The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21, L-carnitine CoA-transferase. The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Roth, S., Jung, K., Jung, H., Hommel, R.K. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(–)-carnitine. Antonie Van Leeuwenhoek 65 (1994) 63–69. [PMID: 8060125] |
2. |
Preusser, A., Wagner, U., Elssner, T. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim. Biophys. Acta 1431 (1999) 166–178. [DOI] [PMID: 10209289] |
3. |
Elssner, T., Hennig, L., Frauendorf, H., Haferburg, D. and Kleber, H.P. Isolation, identification, and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA, compounds involved in carnitine metabolism of E. coli. Biochemistry 39 (2000) 10761–10769. [DOI] [PMID: 10978161] |
4. |
Walt, A. and Kahn, M.L. The fixA and fixB genes are necessary for anaerobic carnitine reduction in Escherichia coli. J. Bacteriol. 184 (2002) 4044–4047. [DOI] [PMID: 12081978] |
|
[EC 1.3.8.13 created 2017] |
|
|
|
|
EC |
1.5.3.10 |
Accepted name: |
dimethylglycine oxidase |
Reaction: |
N,N-dimethylglycine + 5,6,7,8-tetrahydrofolate + O2 = sarcosine + 5,10-methylenetetrahydrofolate + H2O2 |
Other name(s): |
dmg (gene name); N,N-dimethylglycine:oxygen oxidoreductase (demethylating) |
Systematic name: |
N,N-dimethylglycine,5,6,7,8-tetrahydrofolate:oxygen oxidoreductase (demethylating,5,10-methylenetetrahydrofolate-forming) |
Comments: |
A flavoprotein (FAD). The enzyme, characterized from the bacterium Arthrobacter globiformis, contains two active sites connected by a large "reaction chamber". An imine intermediate is transferred between the sites, eliminating the production of toxic formaldehyde. In the absence of folate the enzyme does form formaldehyde. Does not oxidize sarcosine. cf. EC 1.5.8.4, dimethylglycine dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-30-7 |
References: |
1. |
Mori, N., Kawakami, B., Tani, Y. and Yamada, H. Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M-1. Agric. Biol. Chem. 44 (1980) 1383–1389. |
2. |
Meskys, R., Harris, R.J., Casaite, V., Basran, J. and Scrutton, N.S. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268 (2001) 3390–3398. [DOI] [PMID: 11422368] |
3. |
Basran, J., Bhanji, N., Basran, A., Nietlispach, D., Mistry, S., Meskys, R. and Scrutton, N.S. Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry. Biochemistry 41 (2002) 4733–4743. [DOI] [PMID: 11926836] |
4. |
Leys, D., Basran, J. and Scrutton, N.S. Channelling and formation of ‘active’ formaldehyde in dimethylglycine oxidase. EMBO J. 22 (2003) 4038–4048. [DOI] [PMID: 12912903] |
5. |
Basran, J., Fullerton, S., Leys, D. and Scrutton, N.S. Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function. Biochemistry 45 (2006) 11151–11161. [DOI] [PMID: 16964976] |
6. |
Tralau, T., Lafite, P., Levy, C., Combe, J.P., Scrutton, N.S. and Leys, D. An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J. Biol. Chem. 284 (2009) 17826–17834. [DOI] [PMID: 19369258] |
7. |
Casaite, V., Poviloniene, S., Meskiene, R., Rutkiene, R. and Meskys, R. Studies of dimethylglycine oxidase isoenzymes in Arthrobacter globiformis cells. Curr. Microbiol. 62 (2011) 1267–1273. [DOI] [PMID: 21188587] |
|
[EC 1.5.3.10 created 1992, modified 2022] |
|
|
|
|
EC |
1.5.7.3 |
Accepted name: |
N,N-dimethylglycine/sarcosine dehydrogenase (ferredoxin) |
Reaction: |
(1) N,N-dimethylglycine + 2 oxidized ferredoxin + H2O = sarcosine + formaldehyde + 2 reduced ferredoxin + 2 H+ (2) sarcosine + 2 oxidized ferredoxin + H2O = glycine + formaldehyde + 2 reduced ferredoxin + 2 H+ |
Other name(s): |
ddhC (gene name); dgcA (gene name) |
Systematic name: |
N,N-dimethylglycine/sarcosine:ferredoxin oxidoreductase (demethylating) |
Comments: |
This bacterial enzyme is involved in degradation of glycine betaine. The enzyme contains non-covalently bound FAD and NAD(P) cofactors, and catalyses the demethylation of both N,N-dimethylglycine and sarcosine, releasing formaldehyde and forming glycine as the final product. The enzyme can utilize both NAD+ and NADP+, but the catalytic efficiency with NAD+ is ~5-fold higher. The native electron acceptor of the enzyme is a membrane-bound clostridial-type ferredoxin, which transfers the electrons to an electron-transfer flavoprotein (ETF). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wargo, M.J., Szwergold, B.S. and Hogan, D.A. Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism. J. Bacteriol. 190 (2008) 2690–2699. [DOI] [PMID: 17951379] |
2. |
Yang, T., Shao, Y.H., Guo, L.Z., Meng, X.L., Yu, H. and Lu, W.D. Role of N,N-dimethylglycine and its catabolism to sarcosine in Chromohalobacter salexigens DSM 3043. Appl. Environ. Microbiol. 86 (2020) . [DOI] [PMID: 32631860] |
|
[EC 1.5.7.3 created 2022] |
|
|
|
|
EC |
1.13.11.90 |
Accepted name: |
[1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming) |
Reaction: |
[(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate + O2 = glycine betaine + phosphate |
Other name(s): |
tmpB (gene name) |
Systematic name: |
[(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate:oxygen 1R-oxidoreductase (glycine-betaine-forming) |
Comments: |
Requires Fe2+. This bacterial enzyme is involved in a degradation pathway for [2-(trimethylamino)ethyl]phosphonate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rajakovich, L.J., Pandelia, M.E., Mitchell, A.J., Chang, W.C., Zhang, B., Boal, A.K., Krebs, C. and Bollinger, J.M., Jr. A new microbial pathway for organophosphonate degradation catalyzed by two previously misannotated non-heme-iron oxygenases. Biochemistry 58 (2019) 1627–1647. [PMID: 30789718] |
|
[EC 1.13.11.90 created 2020] |
|
|
|
|
EC |
1.14.11.1 |
Accepted name: |
γ-butyrobetaine dioxygenase |
Reaction: |
4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2 |
Other name(s): |
α-butyrobetaine hydroxylase; γ-butyrobetaine hydroxylase; butyrobetaine hydroxylase |
Systematic name: |
4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) |
Comments: |
Requires Fe2+ and ascorbate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-31-2 |
References: |
1. |
Lindstedt, G. and Lindstedt, S. Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver. J. Biol. Chem. 245 (1970) 4178–4186. [PMID: 4396068] |
|
[EC 1.14.11.1 created 1972] |
|
|
|
|
EC |
1.14.13.239 |
Accepted name: |
carnitine monooxygenase |
Reaction: |
L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O |
Glossary: |
(3R)-3-hydroxy-4-oxobutanoate = L-malic semialdehyde |
Other name(s): |
cntAB (gene names); yeaWX (gene names) |
Systematic name: |
L-carnitine,NAD(P)H:oxygen oxidoreductase (trimethylamine-forming) |
Comments: |
The bacterial enzyme is a complex consisting of a reductase and an oxygenase components. The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ditullio, D., Anderson, D., Chen, C.S. and Sih, C.J. L-Carnitine via enzyme-catalyzed oxidative kinetic resolution. Bioorg. Med. Chem. 2 (1994) 415–420. [DOI] [PMID: 8000862] |
2. |
Zhu, Y., Jameson, E., Crosatti, M., Schafer, H., Rajakumar, K., Bugg, T.D. and Chen, Y. Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota. Proc. Natl. Acad. Sci. USA 111 (2014) 4268–4273. [DOI] [PMID: 24591617] |
3. |
Koeth, R.A., Levison, B.S., Culley, M.K., Buffa, J.A., Wang, Z., Gregory, J.C., Org, E., Wu, Y., Li, L., Smith, J.D., Tang, W.H., DiDonato, J.A., Lusis, A.J. and Hazen, S.L. γ-Butyrobetaine is a proatherogenic intermediate in gut microbial metabolism of L-carnitine to TMAO. Cell Metab 20 (2014) 799–812. [DOI] [PMID: 25440057] |
|
[EC 1.14.13.239 created 2017] |
|
|
|
|
EC |
1.14.13.247 |
Accepted name: |
stachydrine N-demethylase |
Reaction: |
L-proline betaine + NAD(P)H + H+ + O2 = N-methyl-L-proline + formaldehyde + NAD(P)+ + H2O |
Other name(s): |
L-proline betaine N-demethylase; stc2 (gene name) |
Systematic name: |
L-proline betaine,NAD(P)H:oxygen oxidoreductase (formaldehyde-forming) |
Comments: |
The enzyme, characterized from the bacterium Sinorhizobium meliloti 1021, consists of three different types of subunits. The catalytic unit contains a Rieske [2Fe-2S] iron-sulfur cluster, and catalyses the monooxygenation of a methyl group. The resulting N-methoxyl group is unstable and decomposes spontaneously to form formaldehyde. The other subunits are involved in the transfer of electrons from NAD(P)H to the catalytic subunit. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Daughtry, K.D., Xiao, Y., Stoner-Ma, D., Cho, E., Orville, A.M., Liu, P. and Allen, K.N. Quaternary ammonium oxidative demethylation: X-ray crystallographic, resonance Raman, and UV-visible spectroscopic analysis of a Rieske-type demethylase. J. Am. Chem. Soc. 134 (2012) 2823–2834. [PMID: 22224443] |
2. |
Kumar, R., Zhao, S., Vetting, M.W., Wood, B.M., Sakai, A., Cho, K., Solbiati, J., Almo, S.C., Sweedler, J.V., Jacobson, M.P., Gerlt, J.A. and Cronan, J.E. Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine. MBio 5 (2014) e00933. [DOI] [PMID: 24520058] |
|
[EC 1.14.13.247 created 2017] |
|
|
|
|
EC |
1.14.13.251 |
Accepted name: |
glycine betaine monooxygenase |
Reaction: |
glycine betaine + NADH + H+ + O2 = N,N-dimethylglycine + formaldehyde + NAD+ + H2O |
Other name(s): |
glycine betaine dioxygenase (incorrect); bmoAB (gene names); gbcAB (gene names) |
Systematic name: |
glycine betaine,NADH:oxygen oxidoreductase (demethylating) |
Comments: |
The enzyme, characterized from the bacteria Pseudomonas aeruginosa and Chromohalobacter salexigens, is involved in a degradation pathway of glycine betaine. It is composed of two subunits - a ferredoxin reductase component that contains FAD, and a terminal oxygenase component that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a nonheme iron centre. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wargo, M.J., Szwergold, B.S. and Hogan, D.A. Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism. J. Bacteriol. 190 (2008) 2690–2699. [DOI] [PMID: 17951379] |
2. |
Li, S., Yu, X. and Beattie, G.A. Glycine betaine catabolism contributes to Pseudomonas syringae tolerance to hyperosmotic stress by relieving betaine-mediated suppression of compatible solute synthesis. J. Bacteriol. 195 (2013) 2415–2423. [DOI] [PMID: 23524610] |
3. |
Shao, Y.H., Guo, L.Z., Zhang, Y.Q., Yu, H., Zhao, B.S., Pang, H.Q. and Lu, W.D. Glycine betaine monooxygenase, an unusual Rieske-type oxygenase system, catalyzes the oxidative N-demethylation of glycine betaine in Chromohalobacter salexigens DSM 3043. Appl. Environ. Microbiol. 84 (2018) . [DOI] [PMID: 29703733] |
|
[EC 1.14.13.251 created 2022] |
|
|
|
|
EC |
1.14.15.7 |
Accepted name: |
choline monooxygenase |
Reaction: |
choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin |
Glossary: |
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium |
Systematic name: |
choline,reduced-ferredoxin:oxygen oxidoreductase |
Comments: |
The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [7]. The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 118390-76-4 |
References: |
1. |
Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322–329. [PMID: 16666757] |
2. |
Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581–588. [PMID: 12228495] |
3. |
Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454–3458. [DOI] [PMID: 9096415] |
4. |
Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859–865. [PMID: 9489025] |
5. |
Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101–110. |
6. |
Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487–496. [DOI] [PMID: 9881168] |
7. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
|
[EC 1.14.15.7 created 2001, modified 2002 (EC 1.14.14.4 created 2000, incorporated 2002), modified 2005, modified 2011] |
|
|
|
|
EC |
1.21.4.2 |
Accepted name: |
glycine reductase |
Reaction: |
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin |
|
For diagram of possible mechanism, click here |
Systematic name: |
acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming) |
Comments: |
The reaction is observed only in the direction of glycine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39307-24-9 |
References: |
1. |
Wagner, M., Sonntag, D., Grimm, R., Pich, A. Eckerskorn, C., Söhling, B. and Andreesen, J.R. Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Eur. J. Biochem. 260 (1999) 38–49. [DOI] [PMID: 10091582] |
2. |
Bednarski, B., Andreesen, J.R. and Pich, A. In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue. Eur. J. Biochem. 268 (2001) 3538–3544. [DOI] [PMID: 11422384] |
|
[EC 1.21.4.2 created 2003] |
|
|
|
|
EC |
1.21.4.3 |
Accepted name: |
sarcosine reductase |
Reaction: |
acetyl phosphate + methylamine + thioredoxin disulfide + H2O = N-methylglycine + phosphate + thioredoxin |
|
For diagram of possible reaction mechanism, click here |
Glossary: |
sarcosine = N-methylglycine |
Systematic name: |
acetyl-phosphate methylamine:thioredoxin disulfide oxidoreductase (N-methylglycine-forming) |
Comments: |
The reaction is observed only in the direction of sarcosine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for sarcosine binding and methylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.4 (betaine reductase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-88-7 |
References: |
1. |
Wagner, M., Sonntag, D., Grimm, R., Pich, A. Eckerskorn, C., Söhling, B. and Andreesen, J.R. Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Eur. J. Biochem. 260 (1999) 38–49. [DOI] [PMID: 10091582] |
2. |
Hormann, K. and Andreesen, J.R. Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase. Arch. Microbiol. 153 (1989) 50–59. |
|
[EC 1.21.4.3 created 2003] |
|
|
|
|
EC |
1.21.4.4 |
Accepted name: |
betaine reductase |
Reaction: |
acetyl phosphate + trimethylamine + thioredoxin disulfide + H2O = betaine + phosphate + thioredoxin |
|
For diagram of possible mechanism, click here |
Glossary: |
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Other name(s): |
acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (N,N,N-trimethylglycine-forming) |
Systematic name: |
acetyl-phosphate trimethylamine:thioredoxin disulfide oxidoreductase (betaine-forming) |
Comments: |
The reaction is observed only in the direction of betaine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for betaine binding and trimethylamine release. Subunit A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.2 (glycine reductase) and EC 1.21.4.3 (sarcosine reductase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 125752-87-6 |
References: |
1. |
Wagner, M., Sonntag, D., Grimm, R., Pich, A. Eckerskorn, C., Söhling, B. and Andreesen, J.R. Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Eur. J. Biochem. 260 (1999) 38–49. [DOI] [PMID: 10091582] |
2. |
Bednarski, B., Andreesen, J.R. and Pich, A. In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue. Eur. J. Biochem. 268 (2001) 3538–3544. [DOI] [PMID: 11422384] |
|
[EC 1.21.4.4 created 2003, modified 2010] |
|
|
|
|
EC |
2.1.1.3 |
Accepted name: |
thetin—homocysteine S-methyltransferase |
Reaction: |
dimethylsulfonioacetate + L-homocysteine = (methylsulfanyl)acetate + L-methionine |
Glossary: |
thetin = sulfobetaine = dimethylsulfonioacetate |
Other name(s): |
dimethylthetin-homocysteine methyltransferase; thetin-homocysteine methylpherase |
Systematic name: |
dimethylsulfonioacetate:L-homocysteine S-methyltransferase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-76-9 |
References: |
1. |
Klee, W.A., Richards, H.H. and Cantoni, G.L. The synthesis of methionine by enzymic transmethylation. VII. Existence of two separate homocysteine methylpherases on mammalian liver. Biochim. Biophys. Acta 54 (1961) 157–164. [DOI] [PMID: 14456704] |
2. |
Maw, G.A. Thetin-homocysteine transmethylase. A preliminary manometric study of the enzyme from rat liver. Biochem. J. 63 (1956) 116–124. [PMID: 13315256] |
3. |
Maw, G.A. Thetin-homocysteine transmethylase. Some further characteristics of the enzyme from rat liver. Biochem. J. 70 (1958) 168–173. [PMID: 13584318] |
|
[EC 2.1.1.3 created 1961] |
|
|
|
|
EC |
2.1.1.5 |
Accepted name: |
betaine—homocysteine S-methyltransferase |
Reaction: |
betaine + L-homocysteine = dimethylglycine + L-methionine |
Glossary: |
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Other name(s): |
betaine-homocysteine methyltransferase; betaine-homocysteine transmethylase |
Systematic name: |
trimethylammonioacetate:L-homocysteine S-methyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-78-1 |
References: |
1. |
Klee, W.A., Richards, H.H. and Cantoni, G.L. The synthesis of methionine by enzymic transmethylation. VII. Existence of two separate homocysteine methylpherases on mammalian liver. Biochim. Biophys. Acta 54 (1961) 157–164. [DOI] [PMID: 14456704] |
|
[EC 2.1.1.5 created 1961] |
|
|
|
|
EC |
2.1.1.156 |
Accepted name: |
glycine/sarcosine N-methyltransferase |
Reaction: |
2 S-adenosyl-L-methionine + glycine = 2 S-adenosyl-L-homocysteine + N,N-dimethylglycine (overall reaction) (1a) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine (1b) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine |
Glossary: |
sarcosine = N-methylglycine |
Other name(s): |
ApGSMT; glycine-sarcosine methyltransferase; GSMT; GMT; glycine sarcosine N-methyltransferase; S-adenosyl-L-methionine:sarcosine N-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:glycine(or sarcosine) N-methyltransferase [sarcosine(or N,N-dimethylglycine)-forming] |
Comments: |
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase. Differs from EC 2.1.1.20, glycine N-methyltransferase, as it can further methylate the product of the first reaction. Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 294210-82-5 |
References: |
1. |
Nyyssölä, A., Kerovuo, J., Kaukinen, P., von Weymarn, N. and Reinikainen, T. Extreme halophiles synthesize betaine from glycine by methylation. J. Biol. Chem. 275 (2000) 22196–22201. [DOI] [PMID: 10896953] |
2. |
Nyyssölä, A., Reinikainen, T. and Leisola, M. Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. Appl. Environ. Microbiol. 67 (2001) 2044–2050. [DOI] [PMID: 11319079] |
3. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
|
[EC 2.1.1.156 created 2005] |
|
|
|
|
EC |
2.1.1.157 |
Accepted name: |
sarcosine/dimethylglycine N-methyltransferase |
Reaction: |
2 S-adenosyl-L-methionine + sarcosine = 2 S-adenosyl-L-homocysteine + betaine (overall reaction) (1a) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine (1b) S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine |
Glossary: |
sarcosine = N-methylglycine
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Other name(s): |
ApDMT; sarcosine-dimethylglycine methyltransferase; SDMT; sarcosine dimethylglycine N-methyltransferase; S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:sarcosine(or N,N-dimethylglycine) N-methyltransferase [N,N-dimethylglycine(or betaine)-forming] |
Comments: |
Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. The first enzyme, EC 2.1.1.156, glycine/sarcosine N-methyltransferase, leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of this enzyme. Both of these enzymes can catalyse the formation of N,N-dimethylglycine from sarcosine [3]. The reactions are strongly inhibited by S-adenosyl-L-homocysteine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Nyyssölä, A., Kerovuo, J., Kaukinen, P., von Weymarn, N. and Reinikainen, T. Extreme halophiles synthesize betaine from glycine by methylation. J. Biol. Chem. 275 (2000) 22196–22201. [DOI] [PMID: 10896953] |
2. |
Nyyssölä, A., Reinikainen, T. and Leisola, M. Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. Appl. Environ. Microbiol. 67 (2001) 2044–2050. [DOI] [PMID: 11319079] |
3. |
Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932–4942. [DOI] [PMID: 12466265] |
|
[EC 2.1.1.157 created 2005, modified 2010] |
|
|
|
|
EC |
2.1.1.161 |
Accepted name: |
dimethylglycine N-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine |
Glossary: |
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Other name(s): |
BsmB; DMT |
Systematic name: |
S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase (betaine-forming) |
Comments: |
This enzyme, from the marine cyanobacterium Synechococcus sp. WH8102, differs from EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase in that it cannot use sarcosine as an alternative substrate [1]. Betaine is a ’compatible solute’ that enables cyanobacteria to cope with osmotic stress by maintaining a positive cellular turgor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lu, W.D., Chi, Z.M. and Su, C.D. Identification of glycine betaine as compatible solute in Synechococcus sp. WH8102 and characterization of its N-methyltransferase genes involved in betaine synthesis. Arch. Microbiol. 186 (2006) 495–506. [DOI] [PMID: 17019606] |
|
[EC 2.1.1.161 created 2007] |
|
|
|
|
EC |
2.1.1.162 |
Accepted name: |
glycine/sarcosine/dimethylglycine N-methyltransferase |
Reaction: |
3 S-adenosyl-L-methionine + glycine = 3 S-adenosyl-L-homocysteine + betaine (overall reaction) (1a) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine (1b) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine (1c) S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine |
Glossary: |
sarcosine = N-methylglycine
betaine = glycine betaine = N,N,N-trimethylglycine = N,N,N-trimethylammonioacetate |
Other name(s): |
GSDMT; glycine sarcosine dimethylglycine N-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:glycine(or sarcosine or N,N-dimethylglycine) N-methyltransferase [sarcosine(or N,N-dimethylglycine or betaine)-forming] |
Comments: |
Unlike EC 2.1.1.156 (glycine/sarcosine N-methyltransferase), EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase) and EC 2.1.1.161 (dimethylglycine N-methyltransferase), this enzyme, from the halophilic methanoarchaeon Methanohalophilus portucalensis, can methylate glycine and all of its intermediates to form the compatible solute betaine [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lai, M.C., Wang, C.C., Chuang, M.J., Wu, Y.C. and Lee, Y.C. Effects of substrate and potassium on the betaine-synthesizing enzyme glycine sarcosine dimethylglycine N-methyltransferase from a halophilic methanoarchaeon Methanohalophilus portucalensis. Res. Microbiol. 157 (2006) 948–955. [DOI] [PMID: 17098399] |
|
[EC 2.1.1.162 created 2007] |
|
|
|
|
EC |
2.1.1.269 |
Accepted name: |
dimethylsulfoniopropionate demethylase |
Reaction: |
S,S-dimethyl-β-propiothetin + tetrahydrofolate = 3-(methylsulfanyl)propanoate + 5-methyltetrahydrofolate |
|
For diagram of 3-(dimethylsulfonio)propanoate metabolism, click here |
Glossary: |
S,S-dimethyl-β-propiothetin = 3-(S,S-dimethylsulfonio)propanoate |
Other name(s): |
dmdA (gene name); dimethylsulfoniopropionate-dependent demethylase A |
Systematic name: |
S,S-dimethyl-β-propiothetin:tetrahydrofolate S-methyltransferase |
Comments: |
The enzyme from the marine bacteria Pelagibacter ubique and Ruegeria pomeroyi are specific towards S,S-dimethyl-β-propiothetin. They do not demethylate glycine-betaine [1,2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Jansen, M. and Hansen, T.A. Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria. Arch. Microbiol. 169 (1998) 84–87. [PMID: 9396840] |
2. |
Reisch, C.R., Moran, M.A. and Whitman, W.B. Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter ubique and Silicibacter pomeroyi. J. Bacteriol. 190 (2008) 8018–8024. [DOI] [PMID: 18849431] |
3. |
Schuller, D.J., Reisch, C.R., Moran, M.A., Whitman, W.B. and Lanzilotta, W.N. Structures of dimethylsulfoniopropionate-dependent demethylase from the marine organism Pelagibacter ubique. Protein Sci. 21 (2012) 289–298. [DOI] [PMID: 22162093] |
|
[EC 2.1.1.269 created 2013] |
|
|
|
|
EC |
2.1.1.376 |
Accepted name: |
glycine betaine—corrinoid protein Co-methyltransferase |
Reaction: |
glycine betaine + a [Co(I) glycine betaine-specific corrinoid protein] = N,N-dimethylglycine + a [methyl-Co(III) glycine betaine-specific corrinoid protein] |
Other name(s): |
mtgB (gene name); glycine betaine methyltransferase |
Systematic name: |
glycine betaine:[Co(I) glycine betaine-specific corrinoid protein] Co-methyltransferase |
Comments: |
The enzyme, which catalyses the transfer of a methyl group from glycine betaine to a glycine betaine-specific corrinoid protein (MtgC), is involved in methanogenesis from glycine betaine in some methanogenic archaea, and in glycine betaine degradation in some bacteria. Unlike similar enzymes involved in methanogenesis from methylated C1 compounds, this enzyme does not contain the unusual amino acid L-pyrrolysine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668–E4676. [DOI] [PMID: 25313086] |
2. |
Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10:2572 (2019). [DOI] [PMID: 31787957] |
|
[EC 2.1.1.376 created 2021] |
|
|
|
|
EC |
2.1.1.377 |
Accepted name: |
[methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase |
Reaction: |
a [methyl-Co(III) glycine betaine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) glycine betaine-specific corrinoid protein] |
Other name(s): |
mtaA (gene name) |
Systematic name: |
methylated glycine betaine-specific corrinoid protein:CoM methyltransferase |
Comments: |
The enzyme, which is involved in methanogenesis from glycine betaine, catalyses the transfer of a methyl group bound to the cobalt cofactor of glycine betaine-specific corrinoid protein to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, which catalyses the final step in methanogenesis. The enzyme from the methanogenic archaeon Methanolobus vulcani B1d can also catalyse the activity of EC 2.1.1.246, [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10:2572 (2019). [DOI] [PMID: 31787957] |
|
[EC 2.1.1.377 created 2021] |
|
|
|
|
EC |
2.1.1.378 |
Accepted name: |
[methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase |
Reaction: |
a [methyl-Co(III) glycine betaine-specific corrinoid protein] + tetrahydrofolate = a [Co(I) glycine betaine-specific corrinoid protein] + 5-methyltetrahydrofolate |
Other name(s): |
mtgA (gene name); DSY3157 (locus name) |
Systematic name: |
[methyl-Co(III) glycine betaine-specific corrinoid protein]:tetrahydrofolate N-methyltransferase |
Comments: |
This enzyme, characterized from the anaerobic bacterium Desulfitobacterium hafniense Y51, catalyses a similar reaction to that of EC 2.1.1.258, 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase, but in the opposite direction, transferring a methyl group from a methylated corrinoid protein to tetrahydrofolate. The corrinoid protein is specifically methylated by EC 2.1.1.376, glycine betaine—corrinoid protein Co-methyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668–E4676. [DOI] [PMID: 25313086] |
|
[EC 2.1.1.378 created 2021] |
|
|
|
|
EC |
2.1.1.388 |
Accepted name: |
proline betaine—corrinoid protein Co-methyltransferase |
Reaction: |
L-proline betaine + a [Co(I) quaternary-amine-specific corrinoid protein] = a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + N-methyl-L-proline |
Glossary: |
L-proline betaine = (2S)-1,1-dimethylpyrrolidinium-2-carboxylate |
Other name(s): |
mtpB (gene name) |
Systematic name: |
L-proline betaine:[Co(I) quaternary-amine-specific corrinoid protein] Co-methyltransferase |
Comments: |
The enzyme, characterized from the bacterium Eubacterium limosum, is a component of a system that transfers a methyl group from L-proline betaine to tetrahydrofolate, as part of an L-proline betaine degradation pathway. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697–13707. [DOI] [PMID: 31341018] |
|
[EC 2.1.1.388 created 2023] |
|
|
|
|
EC |
2.1.1.389 |
Accepted name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]—tetrahydrofolate methyltransferase |
Reaction: |
a [methyl-Co(III) quaternary-amine-specific corrinoid protein] + tetrahydrofolate = N5-methyltetrahydrofolate + a [Co(I) quaternary-amine-specific corrinoid protein] |
Other name(s): |
mtqA (gene name) (ambiguous); [methyl-Co(III) MtqC corrinoid protein]—tetrahydrofolate methyltransferase |
Systematic name: |
[methyl-Co(III) quaternary-amine-specific corrinoid protein]:tetrahydrofolate methyltransferase |
Comments: |
The enzyme, characterized from the acetogenic gut bacterium Eubacterium limosum, participates in a pathway for the degradation of some quaternary amine compounds (L-proline betaine and L-carnitine). The enzyme catalyses the transfer of a methyl group bound to the cobalt cofactor of a dedicated corrinoid protein (bacterial MtqC) to tetrahydrofolate. The resulting 5-methyltetrahydrofolate is processed to acetyl-CoA via the Wood—Ljungdahl pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Picking, J.W., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylation. J. Biol. Chem. 294 (2019) 13697–13707. [DOI] [PMID: 31341018] |
2. |
Kountz, D.J., Behrman, E.J., Zhang, L. and Krzycki, J.A. MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamin-dependent carnitine demethylase. J. Biol. Chem. 295 (2020) 11971–11981. [DOI] [PMID: 32571881] |
|
[EC 2.1.1.389 created 2023] |
|
|
|
|
EC |
2.8.3.21 |
Accepted name: |
L-carnitine CoA-transferase |
Reaction: |
(1) (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA (2) 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA |
Glossary: |
L-carnitine = (3R)-3-hydroxy-4-(trimethylammonio)butanoate
(E)-4-(trimethylammonio)but-2-enoate = crotonobetaine
4-trimethylammoniobutanoate = γ-butyrobetaine |
Other name(s): |
CaiB; crotonobetainyl/γ-butyrobetainyl-CoA:carnitine CoA-transferase |
Systematic name: |
(E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase |
Comments: |
The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545] |
2. |
Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212] |
3. |
Stenmark, P., Gurmu, D. and Nordlund, P. Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism. Biochemistry 43 (2004) 13996–14003. [DOI] [PMID: 15518548] |
4. |
Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894] |
5. |
Rangarajan, E.S., Li, Y., Iannuzzi, P., Cygler, M. and Matte, A. Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA. Biochemistry 44 (2005) 5728–5738. [DOI] [PMID: 15823031] |
|
[EC 2.8.3.21 created 2014] |
|
|
|
|
EC
|
3.6.3.32
|
Transferred entry: | quaternary-amine-transporting ATPase. Now EC 7.6.2.9, quaternary-amine-transporting ATPase
|
[EC 3.6.3.32 created 2000, deleted 2018] |
|
|
|
|
EC |
4.2.1.149 |
Accepted name: |
crotonobetainyl-CoA hydratase |
Reaction: |
L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O |
Glossary: |
L-carnitinyl-CoA = (3R)-3-hydroxy-4-(trimethylammonio)butanoyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA = crotonobetainyl-CoA |
Other name(s): |
CaiD; L-carnityl-CoA dehydratase |
Systematic name: |
L-carnitinyl-CoA hydro-lyase [(E)-4-(trimethylammonio)but-2-enoyl-CoA-forming] |
Comments: |
The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545] |
2. |
Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212] |
3. |
Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894] |
|
[EC 4.2.1.149 created 2014] |
|
|
|
|
EC |
5.1.1.22 |
Accepted name: |
4-hydroxyproline betaine 2-epimerase |
Reaction: |
(1) trans-4-hydroxy-L-proline betaine = cis-4-hydroxy-D-proline betaine (2) L-proline betaine = D-proline betaine |
Glossary: |
trans-4-hydroxy-L-proline betaine = (2S,4R)-4-hydroxy-1,1-dimethylpyrrolidinium-2-carboxylate
cis-4-hydroxy-D-proline betaine = (2R,4R)-4-hydroxy-1,1-dimethylpyrrolidinium-2-carboxylate
L-proline betaine = (2S)-1,1-dimethylpyrrolidinium-2-carboxylate
D-proline betaine = (2R)-1,1-dimethylpyrrolidinium-2-carboxylate |
Other name(s): |
hpbD (gene name); Hyp-B 2-epimerase; (4R)-4-hydroxyproline betaine 2-epimerase |
Systematic name: |
4-hydroxyproline betaine 2-epimerase |
Comments: |
The enzyme, characterized from the bacteria Pelagibaca bermudensis and Paracoccus denitrificans, specifically catalyses racemization of trans-4-hydroxy-L-proline betaine and L-proline betaine at the C-2 position. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Zhao, S., Kumar, R., Sakai, A., Vetting, M.W., Wood, B.M., Brown, S., Bonanno, J.B., Hillerich, B.S., Seidel, R.D., Babbitt, P.C., Almo, S.C., Sweedler, J.V., Gerlt, J.A., Cronan, J.E. and Jacobson, M.P. Discovery of new enzymes and metabolic pathways by using structure and genome context. Nature 502 (2013) 698–702. [DOI] [PMID: 24056934] |
2. |
Kumar, R., Zhao, S., Vetting, M.W., Wood, B.M., Sakai, A., Cho, K., Solbiati, J., Almo, S.C., Sweedler, J.V., Jacobson, M.P., Gerlt, J.A. and Cronan, J.E. Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine. MBio 5 (2014) e00933. [DOI] [PMID: 24520058] |
|
[EC 5.1.1.22 created 2017] |
|
|
|
|
EC |
6.2.1.48 |
Accepted name: |
carnitine—CoA ligase |
Reaction: |
ATP + L-carnitine + CoA = AMP + diphosphate + L-carnitinyl-CoA |
Glossary: |
carnitine = 3-hydroxy-4-(trimethylammonio)butanoate
crotonobetaine = (E)-4-(trimethylammonio)but-2-enoate
γ-butyrobetaine = 4-(trimethylammonio)butanoate |
Other name(s): |
caiC (gene name) |
Systematic name: |
L-carnitine:CoA ligase (AMP-forming) |
Comments: |
The enzyme, originally characterized from the bacterium Escherichia coli, can catalyse the transfer of CoA to L-carnitine, crotonobetaine and γ-butyrobetaine. In vitro the enzyme also exhibits the activity of EC 2.8.3.21, L-carnitine CoA-transferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Eichler, K., Bourgis, F., Buchet, A., Kleber, H.P. and Mandrand-Berthelot, M.A. Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol. Microbiol. 13 (1994) 775–786. [DOI] [PMID: 7815937] |
2. |
Bernal, V., Arense, P., Blatz, V., Mandrand-Berthelot, M.A., Canovas, M. and Iborra, J.L. Role of betaine:CoA ligase (CaiC) in the activation of betaines and the transfer of coenzyme A in Escherichia coli. J. Appl. Microbiol. 105 (2008) 42–50. [DOI] [PMID: 18266698] |
|
[EC 6.2.1.48 created 2017] |
|
|
|
|
EC |
7.6.2.9 |
Accepted name: |
ABC-type quaternary amine transporter |
Reaction: |
ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1] |
Other name(s): |
glycine betaine ABC transporter; ProVWX; quaternary-amine ABC transporter; quaternary-amine-transporting ATPase (ambiguous) |
Systematic name: |
ATP phosphohydrolase (ABC-type, quaternary-amine-importing) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of quaternary amine derivatives. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321] |
2. |
Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213–6220. [DOI] [PMID: 9335265] |
3. |
Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977] |
|
[EC 7.6.2.9 created 2000 as EC 3.6.3.32, transferred 2018 to EC 7.6.2.9] |
|
|
|
|