The Enzyme Database

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EC 1.1.1.75     
Accepted name: (R)-aminopropanol dehydrogenase
Reaction: (R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+
Other name(s): L-aminopropanol dehydrogenase; 1-aminopropan-2-ol-NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase; 1-aminopropan-2-ol-dehydrogenase; DL-1-aminopropan-2-ol: NAD+ dehydrogenase; L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase
Systematic name: (R)-1-aminopropan-2-ol:NAD+ oxidoreductase
Comments: Requires K+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-13-8
References:
1.  Dekker, E.E. and Swain, R.R. Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli. Biochim. Biophys. Acta 158 (1968) 306–307. [DOI] [PMID: 4385233]
2.  Turner, J.M. Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escherichia coli. Biochem. J. 99 (1966) 427–433. [PMID: 5329339]
3.  Turner, J.M. Microbial metabolism of amino ketones. L-1-Aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli. Biochem. J. 104 (1967) 112–121. [PMID: 5340733]
[EC 1.1.1.75 created 1972]
 
 
EC 1.1.1.80     
Accepted name: isopropanol dehydrogenase (NADP+)
Reaction: propan-2-ol + NADP+ = acetone + NADPH + H+
Other name(s): isopropanol dehydrogenase (NADP)
Systematic name: propan-2-ol:NADP+ oxidoreductase
Comments: Also acts on other short-chain secondary alcohols and, slowly, on primary alcohols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-18-3
References:
1.  Hoshino, K. Organism producing isopropanol from acetone. V. Enzymological [studies] on the oxidation-reduction of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 608–615.
2.  Hoshino, K. and Udagawa, K. Organism producing isopropanol from acetone. VI. Isopropanol dehydrogenase and alcohol dehydrogenase of Lactobacillus brevis var. hofuensis. [in Japanese] Nippon Nogei Kagaku Kaishi 34 (1960) 616–619.
[EC 1.1.1.80 created 1972]
 
 
EC 1.14.13.227     
Accepted name: propane 2-monooxygenase
Reaction: propane + NADH + H+ + O2 = propan-2-ol + NAD+ + H2O
Glossary: propan-2-ol = isopropanol
Other name(s): prmABCD (gene names)
Systematic name: propane,NADH:oxygen oxidoreductase (2-hydroxylating)
Comments: The enzyme, characterized from several bacterial strains, is a multicomponent dinuclear iron monooxygenase that includes a hydroxylase, an NADH-dependent reductase, and a coupling protein. The enzyme has several additional activities, including acetone monooxygenase (acetol-forming) and phenol 4-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kotani, T., Yamamoto, T., Yurimoto, H., Sakai, Y. and Kato, N. Propane monooxygenase and NAD+-dependent secondary alcohol dehydrogenase in propane metabolism by Gordonia sp. strain TY-5. J. Bacteriol. 185 (2003) 7120–7128. [DOI] [PMID: 14645271]
2.  Sharp, J.O., Sales, C.M., LeBlanc, J.C., Liu, J., Wood, T.K., Eltis, L.D., Mohn, W.W. and Alvarez-Cohen, L. An inducible propane monooxygenase is responsible for N-nitrosodimethylamine degradation by Rhodococcus sp. strain RHA1. Appl. Environ. Microbiol. 73 (2007) 6930–6938. [DOI] [PMID: 17873074]
3.  Furuya, T., Hirose, S., Osanai, H., Semba, H. and Kino, K. Identification of the monooxygenase gene clusters responsible for the regioselective oxidation of phenol to hydroquinone in mycobacteria. Appl. Environ. Microbiol. 77 (2011) 1214–1220. [DOI] [PMID: 21183637]
[EC 1.14.13.227 created 2016]
 
 
EC 1.14.13.229     
Accepted name: tert-butyl alcohol monooxygenase
Reaction: tert-butyl alcohol + NADPH + H+ + O2 = 2-methylpropane-1,2-diol + NADP+ + H2O
Other name(s): mdpJK (gene names); tert-butanol monooxygenase
Systematic name: tert-butyl alcohol,NADPH:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, is a Rieske nonheme mononuclear iron oxygenase. It can also act, with lower efficiency, on propan-2-ol, converting it to propane-1,2-diol. Depending on the substrate, the enzyme also catalyses EC 1.14.19.48, tert-amyl alcohol desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schafer, F., Breuer, U., Benndorf, D., von Bergen, M., Harms, H. and Muller, R.H. Growth of Aquincola tertiaricarbonis L108 on tert-butyl alcohol leads to the induction of a phthalate dioxygenase-related protein and its associated oxidoreductase subunit. Eng. Life Sci. 7 (2007) 512–519.
2.  Schuster, J., Schafer, F., Hubler, N., Brandt, A., Rosell, M., Hartig, C., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial degradation of tert-amyl alcohol proceeds via hemiterpene 2-methyl-3-buten-2-ol by employing the tertiary alcohol desaturase function of the Rieske nonheme mononuclear iron oxygenase MdpJ. J. Bacteriol. 194 (2012) 972–981. [DOI] [PMID: 22194447]
[EC 1.14.13.229 created 2016]
 
 
EC 3.5.1.90     
Accepted name: adenosylcobinamide hydrolase
Reaction: adenosylcobinamide + H2O = adenosylcobyric acid + (R)-1-aminopropan-2-ol
For diagram of cobinamide salvage pathways, click here
Other name(s): CbiZ; AdoCbi amidohydrolase
Systematic name: adenosylcobinamide amidohydrolase
Comments: Involved in the salvage pathway of cobinamide in archaea. Archaea convert adenosylcobinamide (AdoCbi) into adenosylcobinamide phosphate (AdoCbi-P) in two steps. First, the amidohydrolase activity of CbiZ cleaves off the aminopropanol moiety of AdoCbi yielding adenosylcobyric acid (AdoCby); second, AdoCby is converted into AdoCbi-P by the action of EC 6.3.1.10, adenosylcobinamide-phosphate synthase (CbiB).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 905988-16-1
References:
1.  Woodson, J.D. and Escalante-Semerena, J.C. CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12 precursor cobinamide in archaea. Proc. Natl. Acad. Sci. USA 101 (2004) 3591–3596. [DOI] [PMID: 14990804]
[EC 3.5.1.90 created 2004]
 
 
EC 4.2.3.2     
Accepted name: ethanolamine-phosphate phospho-lyase
Reaction: ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate
Other name(s): O-phosphoethanolamine-phospholyase; amino alcohol O-phosphate phospholyase; O-phosphorylethanol-amine phospho-lyase; ethanolamine-phosphate phospho-lyase (deaminating)
Systematic name: ethanolamine-phosphate phosphate-lyase (deaminating; acetaldehyde-forming)
Comments: A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-88-3
References:
1.  Fleshood, H.L. and Pitot, H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-Phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414–4420. [PMID: 5498429]
2.  Jones, A., Faulkner, A. and Turner, J.M. Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol o-phosphate phospho-lyase in aldehyde formation. Biochem. J. 134 (1973) 959–968. [PMID: 4357716]
[EC 4.2.3.2 created 1972 as EC 4.2.99.7, transferred 2000 to EC 4.2.3.2]
 
 
EC 4.2.3.84     
Accepted name: 10-epi-γ-eudesmol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 10-epi-γ-eudesmol + diphosphate
For diagram of eudesmol and selinene biosynthesis, click here and for diagram of eudesmol biosynthesis, click here
Glossary: 10-epi-γ-eudesmol = 2-[(2R,4aS)-4a,8-dimethyl-1,2,3,4,4a,5,6,7-octahydronaphthalen-2-yl]propan-2-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (10-epi-γ-eudesmol-forming)
Comments: The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% β-eudesmol, 16.8% 10-epi-γ-eudesmol, 10% α-eudesmol, and 5.6% aristolene. cf. EC 4.2.3.68 (β-eudesmol synthase) and EC 4.2.3.85 (α-eudesmol synthase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yu, F., Harada, H., Yamasaki, K., Okamoto, S., Hirase, S., Tanaka, Y., Misawa, N. and Utsumi, R. Isolation and functional characterization of a β-eudesmol synthase, a new sesquiterpene synthase from Zingiber zerumbet Smith. FEBS Lett. 582 (2008) 565–572. [DOI] [PMID: 18242187]
[EC 4.2.3.84 created 2011]
 
 
EC 4.2.3.85     
Accepted name: α-eudesmol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = α-eudesmol + diphosphate
For diagram of eudesmol biosynthesis, click here
Glossary: (-)-α-eudesmol = 2-[(2R,4aR,8aR)-4a,8-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalen-2-yl]propan-2-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (α-eudesmol-forming)
Comments: The recombinant enzyme from ginger (Zingiber zerumbet) gives 62.6% β-eudesmol, 16.8% 10-epi-γ-eudesmol, 10% α-eudesmol, and 5.6% aristolene. cf. EC 4.2.3.68 (β-eudesmol synthase) and EC 4.2.3.84 (10-epi-γ-eudesmol synthase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yu, F., Harada, H., Yamasaki, K., Okamoto, S., Hirase, S., Tanaka, Y., Misawa, N. and Utsumi, R. Isolation and functional characterization of a β-eudesmol synthase, a new sesquiterpene synthase from Zingiber zerumbet Smith. FEBS Lett. 582 (2008) 565–572. [DOI] [PMID: 18242187]
[EC 4.2.3.85 created 2011]
 
 
EC 4.2.3.149     
Accepted name: nephthenol synthase
Reaction: geranylgeranyl diphosphate + H2O = (R)-nephthenol + diphosphate
For diagram of cembrene and related diterpenoids, click here
Glossary: (R)-nephthenol = 2-[(1R,3E,7E,11E)-4,8,12-trimethyltetradeca-3,7,11-trien-1-yl]propan-2-ol
Other name(s): DtcycA (gene name); DtcycB (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [(R)-nephthenol-forming]
Comments: Requires Mg2+. Two isozymes with this activity were isolated from the bacterium Streptomyces sp. SANK 60404. The enzyme encoded by the DtcycA gene also produces cembrene C (see EC 4.2.3.148, cembrene C synthase), while the enzyme encoded by the DtcycB gene also produces (R)-cembrene A and (1S,4E,8E,12E)-2,2,5,9,13-pentamethylcyclopentadeca-4,8,12-trien-1-ol (see EC 4.2.3.150, cembrene A synthase, and EC 4.2.3.151, pentamethylcyclopentadecatrienol synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Meguro, A., Tomita, T., Nishiyama, M. and Kuzuyama, T. Identification and characterization of bacterial diterpene cyclases that synthesize the cembrane skeleton. ChemBioChem 14 (2013) 316–321. [DOI] [PMID: 23386483]
[EC 4.2.3.149 created 2014]
 
 
EC 4.2.3.167     
Accepted name: dolabella-3,7-dien-18-ol synthase
Reaction: geranylgeranyl diphosphate + H2O = (3E,7E)-dolabella-3,7-dien-18-ol + diphosphate
For diagram of biosynthesis of fusicoccane diterpenoids, click here
Glossary: (3E,7E)-dolabella-3,7-dien-18-ol = 2-[(1R,3aR,5E,9E,12aR)-3a,6,10-trimethyl-1,2,3,3a,4,7,8,11,12,12a-decahydrocyclopenta[11]annulen-1-yl]propan-2-ol
Other name(s): TPS20 (gene name)
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase [cyclizing, (3E,7E)-dolabella-3,7-dien-18-ol-forming]
Comments: Isolated from an ecotype of the plant Arabidopsis thaliana from Cape Verde Islands. The enzyme also gives (3E,7E)-dolathalia-3,7,11-triene and traces of other terpenoids. cf. EC 4.2.3.168 dolathalia-3,7,11-triene synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Q., Jia, M., Huh, J.H., Muchlinski, A., Peters, R.J. and Tholl, D. Identification of a dolabellane type diterpene synthase and other root-expressed diterpene synthases in Arabidopsis. Front. Plant Sci. 7:1761 (2016). [DOI] [PMID: 27933080]
[EC 4.2.3.167 created 2017]
 
 
EC 4.2.3.169     
Accepted name: 7-epi-α-eudesmol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = 7-epi-α-eudesmol + diphosphate
For diagram of eudesmol and selinene biosynthesis, click here
Glossary: 7-epi-α-eudesmol = 2-[(2S,4aR,8aR)-4a,8-dimethyl-1,2,3,4,4a,5,6,8a-octahydronaphthalen-2-yl]propan-2-ol
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, 7-epi-α-eudesmol-forming)
Comments: The enzyme, found in the bacterium Streptomyces viridochromogenes, is specific for (2E,6E)-farnesyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rabe, P., Schmitz, T. and Dickschat, J.S. Mechanistic investigations on six bacterial terpene cyclases. Beilstein J. Org. Chem. 12 (2016) 1839–1850. [DOI] [PMID: 27829890]
[EC 4.2.3.169 created 2017]
 
 
EC 4.2.3.204     
Accepted name: valerianol synthase
Reaction: (2E,6E)-farnesyl diphosphate + H2O = valerianol + diphosphate
Glossary: valerianol = 2-[(2R,8R,8aS)-8,8a-dimethyl-1,2,3,4,6,7,8,8a-octahydro-naphthalen-2-yl]-propan-2-ol
Other name(s): ChTPS1 (gene name); CsiTPS8 (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (valerianol-forming)
Comments: The enzyme was characterized from the trees Camellia hiemalis and Camellia sinensis (black tea). The enzyme from Camellia hiemalis produces (2Z,6E)-hedycaryol as a minor product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hattan, J.I., Shindo, K., Sasaki, T., Ohno, F., Tokuda, H., Ishikawa, K. and Misawa, N. Identification of novel sesquiterpene synthase genes that mediate the biosynthesis of valerianol, which was an unknown ingredient of tea. Sci. Rep. 8:12474 (2018). [PMID: 30127518]
[EC 4.2.3.204 created 2019]
 
 
EC 6.3.1.10     
Accepted name: adenosylcobinamide-phosphate synthase
Reaction: (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate = ADP + phosphate + adenosylcobinamide phosphate
(2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol = ADP + phosphate + adenosylcobinamide
For diagram of corrin biosynthesis (part 6), click here
Other name(s): CbiB
Systematic name: adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming)
Comments: One of the substrates for this reaction, (R)-1-aminopropan-2-yl phosphate, is produced by CobD (EC 4.1.1.81, threonine-phosphate decarboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 905988-16-1
References:
1.  Cheong, C.G., Bauer, C.B., Brushaber, K.R., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry 41 (2002) 4798–4808. [DOI] [PMID: 11939774]
2.  Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390–412. [PMID: 12195810]
[EC 6.3.1.10 created 2004]
 
 


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