The Enzyme Database

Your query returned 5 entries.    printer_iconPrintable version



EC 1.2.1.31     
Accepted name: L-aminoadipate-semialdehyde dehydrogenase
Reaction: (S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ (overall reaction)
(1a) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
(1b) (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NAD(P)+ + 2 H2O = L-2-aminoadipate + NAD(P)H + H+
For diagram of lysine catabolism, click here and for diagram of L-Lysine synthesis, click here
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): aminoadipate semialdehyde dehydrogenase; 2-aminoadipate semialdehyde dehydrogenase; α-aminoadipate-semialdehyde dehydrogenase; α-aminoadipate reductase; 2-aminoadipic semialdehyde dehydrogenase; L-α-aminoadipate δ-semialdehyde oxidoreductase; L-α-aminoadipate δ-semialdehyde:NAD+ oxidoreductase; L-α-aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase; L-2-aminoadipate 6-semialdehyde:NAD(P)+ 6-oxidoreductase
Systematic name: (S)-2-amino-6-oxohexanoate:NAD(P)+ 6-oxidoreductase
Comments: (S)-2-amino-6-oxohexanoate undergoes a spontaneous dehydration forming the cyclic (S)-2,3,4,5-tetrahydropyridine-2-carboxylate, which serves as a substrate for the hydrogenation reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-87-2
References:
1.  Calvert, A.F. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. 3. L-α-Aminoadipate δ-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase. J. Biol. Chem. 241 (1966) 409–414. [PMID: 4285660]
2.  Rodwell, V.W. Δ1-piperideine-6-carboxylic acid and α-aminoadipic acid δ-semialdehyde. Method Enzymol 17B (1971) 188–199.
3.  de La Fuente, J.L., Rumbero, A., Martin, J.F. and Liras, P. Δ-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327 (1997) 59–64. [PMID: 9355735]
4.  Fujii, T., Narita, T., Agematu, H., Agata, N. and Isshiki, K. Cloning and characterization of pcd encoding Δ’-piperideine-6-carboxylate dehydrogenase from Flavobacterium lutescens IFO3084. J. Biochem. 128 (2000) 975–982. [PMID: 11098140]
[EC 1.2.1.31 created 1972, modified 2011]
 
 
EC 1.4.1.18     
Accepted name: lysine 6-dehydrogenase
Reaction: L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction)
(1a) L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
(1b) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous)
For diagram of reaction, click here and for diagram of L-lysine synthesis, click here
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): L-lysine ε-dehydrogenase; L-lysine 6-dehydrogenase; LysDH
Systematic name: L-lysine:NAD+ 6-oxidoreductase (deaminating)
Comments: The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 89400-30-6
References:
1.  Misono, H. and Nagasaki, S. Occurrence of L-lysine ε-dehydrogenase in Agrobacterium tumefaciens. J. Bacteriol. 150 (1982) 398–401. [PMID: 6801024]
2.  Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S. Purification and properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. Agric. Biol. Chem. 49 (1985) 2253–2255.
3.  Misono, H., Hashimoto, H., Uehigashi, H., Nagata, S. and Nagasaki, S. Properties of L-lysine ε-dehydrogenase from Agrobacterium tumefaciens. J. Biochem. (Tokyo) 105 (1989) 1002–1008. [PMID: 2768207]
4.  Heydari, M., Ohshima, T., Nunoura-Kominato, N. and Sakuraba, H. Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression. Appl. Environ. Microbiol. 70 (2004) 937–942. [DOI] [PMID: 14766574]
[EC 1.4.1.18 created 1989, modified 2006, modified 2011]
 
 
EC 1.5.3.7     
Accepted name: L-pipecolate oxidase
Reaction: L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2
Glossary: L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
Other name(s): pipecolate oxidase; L-pipecolic acid oxidase
Systematic name: L-pipecolate:oxygen 1,6-oxidoreductase
Comments: The product reacts with water to form (S)-2-amino-6-oxohexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81669-65-0
References:
1.  Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034–1039. [PMID: 6051341]
2.  Kinzel, J.J. and Bhattacharjee, J.K. Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase. J. Bacteriol. 151 (1982) 1073–1077. [PMID: 6809728]
[EC 1.5.3.7 created 1986, modified 2011]
 
 
EC 1.5.99.3     
Accepted name: L-pipecolate dehydrogenase
Reaction: L-pipecolate + acceptor = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): L-pipecolate:(acceptor) 1,6-oxidoreductase
Systematic name: L-pipecolate:acceptor 1,6-oxidoreductase
Comments: The product reacts with water to form (S)-2-amino-6-oxohexanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-63-5
References:
1.  Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034–1039. [PMID: 6051341]
[EC 1.5.99.3 created 1972, modified 1986, modified 2011]
 
 
EC 2.6.1.36     
Accepted name: L-lysine 6-transaminase
Reaction: L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate
Glossary: (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate
Other name(s): lysine 6-aminotransferase; lysine ε-aminotransferase; lysine ε-transaminase; lysine:2-ketoglutarate 6-aminotransferase; L-lysine-α-ketoglutarate aminotransferase; L-lysine-α-ketoglutarate 6-aminotransferase
Systematic name: L-lysine:2-oxoglutarate 6-aminotransferase
Comments: A pyridoxal-phosphate protein. The product (L-allysine) is converted into the intramolecularly dehydrated form, (S)-2,3,4,5-tetrahydropyridine-2-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-68-6
References:
1.  Soda, K., Misono, H. and Yamamoto, T. L-Lysine:α-ketoglutarate aminotransferase. I. Identification of a product, δ-1-piperideine-6-carboxylic acid. Biochemistry 7 (1968) 4102–4109. [PMID: 5722275]
2.  Soda, K. and Misono, H. L-Lysine: α-ketoglutarate aminotransferase. II. Purification, crystallization, and properties. Biochemistry 7 (1968) 4110–4119. [PMID: 5722276]
[EC 2.6.1.36 created 1972, modified 2011]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald