The Enzyme Database

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EC 1.2.1.19     
Accepted name: aminobutyraldehyde dehydrogenase
Reaction: 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
For diagram of arginine catabolism, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW
Systematic name: 4-aminobutanal:NAD+ 1-oxidoreductase
Comments: The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-98-2
References:
1.  Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737–1741. [PMID: 4817964]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
3.  Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145–2150. [PMID: 13673029]
4.  Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654–657. [PMID: 16663901]
5.  Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016.
6.  Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672]
7.  Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161–1168. [DOI] [PMID: 3129020]
8.  Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116]
9.  Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29–41. [DOI] [PMID: 15381418]
[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]
 
 
EC 1.2.1.88     
Accepted name: L-glutamate γ-semialdehyde dehydrogenase
Reaction: L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
For diagram of reaction, click here
Glossary: L-glutamate 5-semialdehyde = L-glutamate γ-semialdehyde = (S)-2-amino-5-oxopentanoate
Other name(s): 1-pyrroline-5-carboxylate dehydrogenase; Δ1-pyrroline-5-carboxylate dehydrogenase; 1-pyrroline dehydrogenase; pyrroline-5-carboxylate dehydrogenase; pyrroline-5-carboxylic acid dehydrogenase; L-pyrroline-5-carboxylate-NAD+ oxidoreductase; 1-pyrroline-5-carboxylate:NAD+ oxidoreductase; Δ1-pyrroline-5-carboxylic acid dehydrogenase
Systematic name: L-glutamate γ-semialdehyde:NAD+ oxidoreductase
Comments: This enzyme catalyses the irreversible oxidation of glutamate-γ-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate γ-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-82-4
References:
1.  Adams, E. and Goldstone, A. Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3504–3512. [PMID: 13681370]
2.  Strecker, H.J. The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase. J. Biol. Chem. 235 (1960) 3218–3223.
3.  Forlani, G., Scainelli, D. and Nielsen, E. Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato (purification and properties). Plant Physiol. 113 (1997) 1413–1418. [PMID: 12223682]
4.  Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086–13092. [PMID: 1618807]
5.  Inagaki, E., Ohshima, N., Sakamoto, K., Babayeva, N.D., Kato, H., Yokoyama, S. and Tahirov, T.H. New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 462–465. [DOI] [PMID: 17554163]
[EC 1.2.1.88 created 1972 as EC 1.5.1.12, modified 2008, transferred 2013 to EC 1.2.1.88]
 
 
EC 1.4.1.12     
Accepted name: 2,4-diaminopentanoate dehydrogenase
Reaction: (2R,4S)-2,4-diaminopentanoate + H2O + NAD(P)+ = (2R)-2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+
Other name(s): 2,4-diaminopentanoic acid C4 dehydrogenase
Systematic name: (2R,4S)-2,4-diaminopentanoate:NAD(P)+ oxidoreductase (deaminating)
Comments: Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate. It has equal activity with NAD+ and NADP+ [cf. EC 1.4.1.26, 2,4-diaminopentanoate dehydrogenase (NAD+)].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 39346-26-4
References:
1.  Somack, R. and Costilow, R.N. 2,4-Diaminopentanoic acid C4 dehydrogenase. Purification and properties of the protein. J. Biol. Chem. 248 (1973) 385–388. [PMID: 4684685]
2.  Stadtman, T.C. Lysine metabolism by clostridia. XIIB 2,4-Diaminohexanoate dehydrogenase (2,4-diaminopentanoate dehydrogenase). Adv. Enzymol. Relat. Areas Mol. Biol. 38 (1973) 441–445.
3.  Tsuda, Y. and Friedmann, H.C. Ornithine metabolism by Clostridium sticklandii. Oxidation of ornithine to 2-amino-4-ketopentanoic acid via 2,4-diaminopentanoic acid; participation of B12 coenzyme, pyridoxal phosphate, and pyridine nucleotide. J. Biol. Chem. 245 (1970) 5914–5926. [PMID: 4394942]
[EC 1.4.1.12 created 1976, modified 2017]
 
 
EC 1.4.3.10     
Accepted name: putrescine oxidase
Reaction: putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2
Glossary: putrescine = butane-1,4-diamine
Systematic name: putrescine:oxygen oxidoreductase (deaminating)
Comments: A flavoprotein (FAD). 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-87-3
References:
1.  DeSa, R.J. Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme. J. Biol. Chem. 247 (1972) 5527–5534. [PMID: 4341347]
2.  Yamada, H. Putrescine oxidase (Micrococcus rubens). Methods Enzymol. 17B (1971) 726–730.
[EC 1.4.3.10 created 1976]
 
 
EC 1.5.1.1     
Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]
Reaction: (1) L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+
(2) L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Other name(s): Δ1-pyrroline-2-carboxylate reductase; DELTA1-pyrroline-2-carboxylate reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); AbLhpI; pyrroline-2-carboxylate reductase; L-proline:NAD(P)+ 2-oxidoreductase
Systematic name: L-pipecolate/L-proline:NAD(P)+ 2-oxidoreductase
Comments: The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-16-7
References:
1.  Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789–800. [PMID: 13502341]
2.  Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240–250. [DOI] [PMID: 24649405]
[EC 1.5.1.1 created 1961, modified 2015]
 
 
EC 1.5.1.2     
Accepted name: pyrroline-5-carboxylate reductase
Reaction: L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H + H+
For diagram of proline biosynthesis, click here
Other name(s): proline oxidase; L-proline oxidase; 1-pyrroline-5-carboxylate reductase; NADPH-L-Δ1-pyrroline carboxylic acid reductase; L-proline-NAD(P)+ 5-oxidoreductase
Systematic name: L-proline:NAD(P)+ 5-oxidoreductase
Comments: Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-17-8
References:
1.  Adams, E. and Goldstone, A. Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Δ1-pyrroline-3-hydroxy-5-carboxylate. J. Biol. Chem. 235 (1960) 3499–3503. [PMID: 13681369]
2.  Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789–800. [PMID: 13502341]
3.  Smith, M.E. and Greenberg, D.M. Characterization of an enzyme reducing pyrroline-5-carboxylate to proline. Nature (Lond.) 177 (1956) 1130. [PMID: 13334497]
4.  Yura, T. and Vogel, H.J. Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties. J. Biol. Chem. 234 (1959) 335–338. [PMID: 13630905]
[EC 1.5.1.2 created 1961]
 
 
EC 1.5.1.12      
Transferred entry: 1-pyrroline-5-carboxylate dehydrogenase. Now EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase.
[EC 1.5.1.12 created 1972, modified 2008, deleted 2013]
 
 
EC 1.5.1.21     
Accepted name: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)
Reaction: (1) L-pipecolate + NADP+ = 1-piperideine-2-carboxylate + NADPH + H+
(2) L-proline + NADP+ = 1-pyrroline-2-carboxylate + NADPH + H+
Glossary: 1-piperideine-2-carboxylate = 3,4,5,6-tetrahydropyridine-2-carboxylate
Other name(s): Pyr2C reductase; 1,2-didehydropipecolate reductase; P2C reductase; 1,2-didehydropipecolic reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); L-pipecolate:NADP+ 2-oxidoreductase; DELTA1-piperideine-2-carboxylate reductase; Δ1-piperideine-2-carboxylate reductase
Systematic name: L-pipecolate/L-proline:NADP+ 2-oxidoreductase
Comments: The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 52037-88-4
References:
1.  Payton, C.W. and Chang, Y.-F. Δ1-Piperideine-2-carboxylate reductase of Pseudomonas putida. J. Bacteriol. 149 (1982) 864–871. [PMID: 6801013]
2.  Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. and Esaki, N. The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent Δ1-piperideine-2-carboxylate/Δ1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. J. Biol. Chem. 280 (2005) 5329–5335. [DOI] [PMID: 15561717]
3.  Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240–250. [DOI] [PMID: 24649405]
[EC 1.5.1.21 created 1984 (EC 1.5.1.14 created 1976, incorporated 1989), modified 2015]
 
 
EC 1.5.1.35      
Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible
[EC 1.5.1.35 created 2006, deleted 2007]
 
 
EC 1.5.1.48     
Accepted name: 2-methyl-1-pyrroline reductase
Reaction: (R)-2-methylpyrrolidine + NADP+ = 2-methyl-1-pyrroline + NADPH + H+
Other name(s): (R)-imine reductase (ambiguous)
Systematic name: (R)-2-methylpyrrolidine:NADP+ 2-oxidoreductase
Comments: The enzyme from the bacterium Streptomyces sp. GF3587 is highly specific for its substrate and forms only the (R) isomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Mitsukura, K., Suzuki, M., Shinoda, S., Kuramoto, T., Yoshida, T. and Nagasawa, T. Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587. Biosci. Biotechnol. Biochem. 75 (2011) 1778–1782. [DOI] [PMID: 21897027]
[EC 1.5.1.48 created 2014]
 
 
EC 1.5.1.49     
Accepted name: 1-pyrroline-2-carboxylate reductase [NAD(P)H]
Reaction: L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
Systematic name: L-proline:NAD(P)+ 2-oxidoreductase
Comments: The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter. While the enzyme is active with both NADH and NADPH, activity is higher with NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ1-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240–250. [DOI] [PMID: 24649405]
[EC 1.5.1.49 created 2015]
 
 
EC 1.5.5.2     
Accepted name: proline dehydrogenase
Reaction: L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Other name(s): L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase
Systematic name: L-proline:quinone oxidoreductase
Comments: A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9050-70-8
References:
1.  Scarpulla, R.C. and Sofer, R.L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J. Biol. Chem. 253 (1978) 5997–6001. [PMID: 355248]
2.  Brown, E.D. and Wood, J.M. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267 (1992) 13086–13092. [PMID: 1618807]
3.  Moxley, M.A., Tanner, J.J. and Becker, D.F. Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516 (2011) 113–120. [DOI] [PMID: 22040654]
[EC 1.5.5.2 created 1980 as EC 1.5.99.8, transferred 2013 to EC 1.5.5.2]
 
 
EC 1.5.5.3     
Accepted name: hydroxyproline dehydrogenase
Reaction: trans-4-hydroxy-L-proline + a quinone = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + a quinol
Other name(s): HYPDH; OH-POX; hydroxyproline oxidase; PRODH2 (gene name)
Systematic name: trans-4-hydroxy-L-proline:quinone oxidoreductase
Comments: A flavoprotein (FAD). The enzyme from human also has low activity with L-proline (cf. EC 1.5.5.2, proline dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cooper, S.K., Pandhare, J., Donald, S.P. and Phang, J.M. A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species. J. Biol. Chem. 283 (2008) 10485–10492. [DOI] [PMID: 18287100]
2.  Summitt, C.B., Johnson, L.C., Jonsson, T.J., Parsonage, D., Holmes, R.P. and Lowther, W.T. Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. Biochem. J. 466 (2015) 273–281. [DOI] [PMID: 25697095]
[EC 1.5.5.3 created 2017]
 
 
EC 1.5.99.6     
Accepted name: spermidine dehydrogenase
Reaction: spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
Other name(s): spermidine:(acceptor) oxidoreductase
Systematic name: spermidine:acceptor oxidoreductase
Comments: A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-64-6
References:
1.  Tabor, C.W. and Kellogg, P.D. Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. Biol. Chem. 245 (1970) 5424–5433. [PMID: 4918845]
2.  Tabor, H. and Tabor, C.W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 225–226.
[EC 1.5.99.6 created 1976]
 
 
EC 1.5.99.8      
Transferred entry: proline dehydrogenase. Now EC 1.5.5.2, proline dehydrogenase.
[EC 1.5.99.8 created 1980, deleted 2013]
 
 
EC 1.5.99.13     
Accepted name: D-proline dehydrogenase
Reaction: D-proline + acceptor = 1-pyrroline-2-carboxylate + reduced acceptor
Other name(s): D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase
Systematic name: D-proline:acceptor oxidoreductase
Comments: A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal. Chim. Acta 619 (2008) 215–220. [DOI] [PMID: 18558115]
2.  Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861–12867. [DOI] [PMID: 11823469]
[EC 1.5.99.13 created 2010, modified 2011]
 
 
EC 1.13.12.19     
Accepted name: 2-oxoglutarate dioxygenase (ethene-forming)
Reaction: 2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
Glossary: ethene = ethylene
Other name(s): ethylene-forming enzyme; EFE; 2-oxoglutarate dioxygenase (ethylene-forming); 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming)
Systematic name: 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethene-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and 5-hydroxy-L-arginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.The enzymes catalyse two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281–2286. [DOI] [PMID: 1770346]
2.  Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483–489. [DOI] [PMID: 1445291]
3.  Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826–832. [DOI] [PMID: 1445325]
[EC 1.13.12.19 created 2011]
 
 
EC 1.14.11.34      
Transferred entry: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming). Now EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
[EC 1.14.11.34 created 2011, deleted 2018]
 
 
EC 1.14.11.41     
Accepted name: L-arginine hydroxylase
Reaction: L-arginine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-arginine + succinate + CO2
Other name(s): VioC (ambiguous); L-arginine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Fe2+-dependent enzyme. The enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin. It differs from EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming), because it does not form guanidine and (S)-1-pyrroline-5-carboxylate from 3-hydroxy-L-arginine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ju, J., Ozanick, S.G., Shen, B. and Thomas, M.G. Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861. ChemBioChem 5 (2004) 1281–1285. [DOI] [PMID: 15368582]
2.  Helmetag, V., Samel, S.A., Thomas, M.G., Marahiel, M.A. and Essen, L.O. Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis. FEBS J. 276 (2009) 3669–3682. [DOI] [PMID: 19490124]
[EC 1.14.11.41 created 2013]
 
 
EC 1.14.20.7     
Accepted name: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
Reaction: L-arginine + 2-oxoglutarate + O2 = L-glutamate 5-semialdehyde + guanidine + succinate + CO2 (overall reaction)
(1a) L-arginine + 2-oxoglutarate + O2 = 5-hydroxy-L-arginine + succinate + CO2
(1b) 5-hydroxy-L-arginine = L-glutamate 5-semialdehyde + guanidine
Other name(s): ethene-forming enzyme; ethylene-forming enzyme; EFE
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene (ethylene) production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide.The enzyme catalyses two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1. The product of the enzyme, L-glutamate 5-semialdehyde, exists in equilibrium with the cyclic form (S)-1-pyrroline-5-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281–2286. [DOI] [PMID: 1770346]
2.  Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483–489. [DOI] [PMID: 1445291]
3.  Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826–832. [DOI] [PMID: 1445325]
4.  Martinez, S., Fellner, M., Herr, C.Q., Ritchie, A., Hu, J. and Hausinger, R.P. Structures and mechanisms of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme: substrate binding creates a twist. J. Am. Chem. Soc. 139 (2017) 11980–11988. [DOI] [PMID: 28780854]
[EC 1.14.20.7 created 2011 as EC 1.14.11.34, transferred 2018 to EC 1.14.20.7, modified 2023]
 
 
EC 2.3.1.226     
Accepted name: carboxymethylproline synthase
Reaction: malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2
Other name(s): CarB (ambiguous)
Systematic name: malonyl-CoA:(S)-1-pyrroline-5-carboxylate malonyltransferase (cyclizing)
Comments: The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sleeman, M.C. and Schofield, C.J. Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. J. Biol. Chem. 279 (2004) 6730–6736. [DOI] [PMID: 14625287]
2.  Gerratana, B., Arnett, S.O., Stapon, A. and Townsend, C.A. Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily. Biochemistry 43 (2004) 15936–15945. [DOI] [PMID: 15595850]
3.  Sorensen, J.L., Sleeman, M.C. and Schofield, C.J. Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB)—implications for carbapenem biosynthesis. Chem. Commun. (Camb.) (2005) 1155–1157. [DOI] [PMID: 15726176]
4.  Sleeman, M.C., Sorensen, J.L., Batchelar, E.T., McDonough, M.A. and Schofield, C.J. Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis. J. Biol. Chem. 280 (2005) 34956–34965. [DOI] [PMID: 16096274]
5.  Batchelar, E.T., Hamed, R.B., Ducho, C., Claridge, T.D., Edelmann, M.J., Kessler, B. and Schofield, C.J. Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily. Angew. Chem. Int. Ed. Engl. 47 (2008) 9322–9325. [DOI] [PMID: 18972478]
6.  Hamed, R.B., Gomez-Castellanos, J.R., Thalhammer, A., Harding, D., Ducho, C., Claridge, T.D. and Schofield, C.J. Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases. Nat. Chem. 3 (2011) 365–371. [DOI] [PMID: 21505494]
[EC 2.3.1.226 created 2013]
 
 
EC 2.3.1.271     
Accepted name: L-glutamate-5-semialdehyde N-acetyltransferase
Reaction: acetyl-CoA + L-glutamate 5-semialdehyde = CoA + N-acetyl-L-glutamate 5-semialdehyde
Other name(s): MPR1 (gene name); MPR2 (gene name)
Systematic name: acetyl-CoA:L-glutamate-5-semialdehyde N-acetyltransferase
Comments: The enzyme, characterized from the yeast Saccharomyces cerevisiae Σ1278b, N-acetylates L-glutamate 5-semialdehyde, an L-proline biosynthesis/utilization intermediate, into N-acetyl-L-glutamate 5-semialdehyde, an intermediate of L-arginine biosynthesis, under oxidative stress conditions. Its activity results in conversion of L-proline to L-arginine, and reduction in the concentration of L-glutamate 5-semialdehyde and its equilibrium partner, (S)-1-pyrroline-5-carboxylate, which has been linked to production of reactive oxygen species stress. The enzyme also acts on (S)-1-acetylazetidine-2-carboxylate, a toxic L-proline analog produced by some plants, resulting in its detoxification and conferring resistance on the yeast.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Shichiri, M., Hoshikawa, C., Nakamori, S. and Takagi, H. A novel acetyltransferase found in Saccharomyces cerevisiae Σ1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid. J. Biol. Chem. 276 (2001) 41998–42002. [DOI] [PMID: 11555637]
2.  Nomura, M. and Takagi, H. Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate. Proc. Natl. Acad. Sci. USA 101 (2004) 12616–12621. [PMID: 15308773]
3.  Nishimura, A., Kotani, T., Sasano, Y. and Takagi, H. An antioxidative mechanism mediated by the yeast N-acetyltransferase Mpr1: oxidative stress-induced arginine synthesis and its physiological role. FEMS Yeast Res. 10 (2010) 687–698. [DOI] [PMID: 20550582]
4.  Nishimura, A., Nasuno, R. and Takagi, H. The proline metabolism intermediate Δ1-pyrroline-5-carboxylate directly inhibits the mitochondrial respiration in budding yeast. FEBS Lett. 586 (2012) 2411–2416. [DOI] [PMID: 22698729]
5.  Nasuno, R., Hirano, Y., Itoh, T., Hakoshima, T., Hibi, T. and Takagi, H. Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism. Proc. Natl. Acad. Sci. USA 110 (2013) 11821–11826. [DOI] [PMID: 23818613]
[EC 2.3.1.271 created 2018]
 
 
EC 2.6.1.82     
Accepted name: putrescine—2-oxoglutarate transaminase
Reaction: putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
For diagram of arginine catabolism, click here
Glossary: putrescine = butane-1,4-diamine
1-pyrroline = 3,4-dihydro-2H-pyrrole
Other name(s): putrescine-α-ketoglutarate transaminase; YgjG; putrescine:α-ketoglutarate aminotransferase; PAT (ambiguous); putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous); butane-1,4-diamine:2-oxoglutarate aminotransferase
Systematic name: putrescine:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 98982-73-1
References:
1.  Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [DOI] [PMID: 3510672]
2.  Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [DOI] [PMID: 16023116]
3.  Samsonova, N.N., Smirnov, S.V., Altman, I.B. and Ptitsyn, L.R. Molecular cloning and characterization of Escherichia coli K12 ygjG gene. BMC Microbiol. 3 (2003) 2. [DOI] [PMID: 12617754]
[EC 2.6.1.82 created 2006, modified 2017, modified 2021]
 
 
EC 3.5.4.22     
Accepted name: 1-pyrroline-4-hydroxy-2-carboxylate deaminase
Reaction: 1-pyrroline-4-hydroxy-2-carboxylate + H2O = 2,5-dioxopentanoate + NH3
Other name(s): HPC deaminase; 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing)
Systematic name: 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-77-7
References:
1.  Singh, R.M.M. and Adams, E. Enzymatic deamination of Δ1-pyrroline-4-hydroxy-2-carboxylate to 2,5-dioxovalerate (α-ketoglutaric semialdehyde). J. Biol. Chem. 240 (1965) 4344–4351. [PMID: 5845838]
2.  Singh, R.M.M. and Adams, E. Isolation and identification of 2,5-dioxovalerate, an intermediate in the bacterial oxidation of hydroxyproline. J. Biol. Chem. 240 (1965) 4352–4356. [PMID: 5845839]
[EC 3.5.4.22 created 1976]
 
 
EC 4.2.1.77     
Accepted name: trans-L-3-hydroxyproline dehydratase
Reaction: trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O
Other name(s): trans-L-3-hydroxyproline hydro-lyase
Systematic name: trans-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)
Comments: Highly specific.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ramaswamy, S.G. Conversion of 3-hydroxyproline to proline in the rat requires reduced pyridine-nucleotides. Fed. Proc. 42 (1983) 2232.
2.  Visser, W.F., Verhoeven-Duif, N.M. and de Koning, T.J. Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes. J. Biol. Chem. 287 (2012) 21654–21662. [DOI] [PMID: 22528483]
[EC 4.2.1.77 created 1984]
 
 
EC 4.2.1.171     
Accepted name: cis-L-3-hydroxyproline dehydratase
Reaction: cis-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O
Glossary: 1-pyrroline-2-carboxylate = 4,5-dihydro-3H-pyrrole-2-carboxylate
Other name(s): cis-L-3-hydroxyproline hydro-lyase; c3LHypD
Systematic name: cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zhang, X., Kumar, R., Vetting, M.W., Zhao, S., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. A unique cis-3-hydroxy-L-proline dehydratase in the enolase superfamily. J. Am. Chem. Soc. 137 (2015) 1388–1391. [DOI] [PMID: 25608448]
[EC 4.2.1.171 created 2017]
 
 
EC 4.2.1.172     
Accepted name: trans-4-hydroxy-L-proline dehydratase
Reaction: trans-4-hydroxy-L-proline = (S)-1-pyrroline-5-carboxylate + H2O
Glossary: 1-pyrroline = 3,4-dihydro-2H-pyrrole
Systematic name: trans-4-hydroxy-L-proline hydro-lyase
Comments: The enzyme has been characterized from the bacterium Peptoclostridium difficile. The active form contains a glycyl radical that is generated by a dedicated activating enzyme via chemistry involving S-adenosyl-L-methionine (SAM) and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Levin, B.J., Huang, Y.Y., Peck, S.C., Wei, Y., Martinez-Del Campo, A., Marks, J.A., Franzosa, E.A., Huttenhower, C. and Balskus, E.P. A prominent glycyl radical enzyme in human gut microbiomes metabolizes trans-4-hydroxy-L-proline. Science 355 (2017) . [DOI] [PMID: 28183913]
[EC 4.2.1.172 created 2017]
 
 


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