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1.2.1.20

Accepted name:

glutarate-semialdehyde dehydrogenase

Reaction:

5-oxopentanoate + NADP⁺ + H₂O = glutarate + NADPH + H⁺

Glossary:

5-oxopentanoate = glutarate semialdehyde

Other name(s):

glutarate semialdehyde dehydrogenase; davD (gene name)

Systematic name:

glutarate-semialdehyde:NADP⁺ oxidoreductase

Comments:

The enzyme, characterized from multiple Pseudomonas strains, participates in L-lysine degradation. Unlike earlier claims, it prefers NADP⁺ to NAD⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-99-3

References:

1.	Ichihara, A. and Ichihara, E.A. Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase. J. Biochem. (Tokyo) 49 (1961) 154–157. [PMID: 13717359]
2.	Chang, Y. F. and Adams, E. Glutaric semialdehyde dehydrogenase (Pseudomonas putida). Methods Enzymol. 17B (1971) 166–171. [DOI]
3.	Fothergill, J.C. and Guest, J.R. Catabolism of L-lysine by Pseudomonas aeruginosa. J. Gen. Microbiol. 99 (1977) 139–155. [DOI] [PMID: 405455]
4.	Chang, Y.F. and Adams, E. Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism. J. Biol. Chem. 252 (1977) 7979–7986. [PMID: 914857]
5.	Yamanishi, Y., Mihara, H., Osaki, M., Muramatsu, H., Esaki, N., Sato, T., Hizukuri, Y., Goto, S. and Kanehisa, M. Prediction of missing enzyme genes in a bacterial metabolic network. Reconstruction of the lysine-degradation pathway of Pseudomonas aeruginosa. FEBS J. 274 (2007) 2262–2273. [DOI] [PMID: 17388807]

[EC 1.2.1.20 created 1965, modified 2021]

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]

2.6.1.48

Accepted name:

5-aminovalerate transaminase

Reaction:

5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate

Other name(s):

5-aminovalerate aminotransferase; δ-aminovalerate aminotransferase; δ-aminovalerate transaminase

Systematic name:

5-aminopentanoate:2-oxoglutarate aminotransferase

Comments:

A pyridoxal-phosphate protein.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-97-7

References:

1.	Ichihara, A., Ichihara, E.A. and Suda, M. Metabolism of L-lysine by bacterial enzymes. IV. δ-Aminovaleric acid-glutamic acid transaminase. J. Biochem. (Tokyo) 48 (1960) 412–420.

[EC 2.6.1.48 created 1972]

5.4.3.8

Accepted name:

glutamate-1-semialdehyde 2,1-aminomutase

Reaction:

L-glutamate 1-semialdehyde = 5-aminolevulinate

For diagram of the early stages of porphyrin biosynthesis, click here and for mechanism of reaction, click here

Glossary:

L-glutamate 1-semialdehyde = (S)-4-amino-5-oxopentanoate

Other name(s):

glutamate-1-semialdehyde aminotransferase

Systematic name:

(S)-4-amino-5-oxopentanoate 4,5-aminomutase

Comments:

Requires pyridoxal phosphate.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68518-07-0

References:

1.	Gough, S.P. and Kannangara, C.G. Biosynthesis of δ-aminolevulinate in greening barley leaves: glutamate 1-semialdehyde aminotransferase. Carlsberg Res. Commun. 43 (1978) 185–194.

[EC 5.4.3.8 created 1983]