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+ |
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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] |
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[EC 1.2.1.31 created 1972, modified 2011] |
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EC |
1.2.1.95 |
Accepted name: |
L-2-aminoadipate reductase |
Reaction: |
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + H+ + ATP (overall reaction) (1a) L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + AMP + diphosphate = L-2-aminoadipate + holo-[LYS2 peptidyl-carrier-protein] + ATP (1b) (S)-2-amino-6-oxohexanoate + holo-[LYS2 peptidyl-carrier-protein] + NADP+ = L-2-aminoadipyl-[LYS2 peptidyl-carrier-protein] + NADPH + H+ |
Glossary: |
L-2-aminoadipate = (2S)-2-aminohexanedioate |
Other name(s): |
LYS2; α-aminoadipate reductase |
Systematic name: |
(S)-2-amino-6-oxohexanoate:NADP+ oxidoreductase (ATP-forming) |
Comments: |
This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ehmann, D.E., Gehring, A.M. and Walsh, C.T. Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of α-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38 (1999) 6171–6177. [DOI] [PMID: 10320345] |
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[EC 1.2.1.95 created 2015] |
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EC |
1.2.1.103 |
Accepted name: |
[amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase |
Reaction: |
an [amino-group carrier protein]-C-terminal-[N-(1-carboxy-5-oxopentyl)-L-glutamine] + phosphate + NADP+ = an [amino-group carrier protein]-C-terminal-[N-(1-carboxy-5-phosphooxy-5-oxopentyl)-L-glutamine] + NADPH + H+ |
Other name(s): |
lysY (gene name) |
Systematic name: |
[amino-group carrier protein]-C-terminal-[N-(1-carboxy-5-oxopentyl)-L-glutamine]:NADP+ 5-oxidoreductase (phosphorylating) |
Comments: |
The enzyme participates in an L-lysine biosynthesis in certain species of archaea and bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T. and Yamane, H. A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res. 9 (1999) 1175–1183. [PMID: 10613839] |
2. |
Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673–679. [DOI] [PMID: 19620981] |
3. |
Shimizu, T., Tomita, T., Kuzuyama, T. and Nishiyama, M. Crystal Structure of the LysY.LysW Complex from Thermus thermophilus. J. Biol. Chem. 291 (2016) 9948–9959. [PMID: 26966182] |
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[EC 1.2.1.103 created 2019] |
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EC |
1.2.1.106 |
Accepted name: |
[amino-group carrier protein]-5-phospho-L-glutamate reductase |
Reaction: |
an [amino-group carrier protein]-C-terminal-γ-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate + phosphate + NADP+ = an [amino-group carrier protein]-C-terminal-γ-(5-phospho-L-glutamyl)-L-glutamate + NADPH + H+ |
Other name(s): |
lysY (gene name) |
Systematic name: |
[amino-group carrier protein]-C-terminal-γ-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate:NADP+ 5-oxidoreductase (phosphorylating) |
Comments: |
The enzyme participates in an L-arginine biosynthesis pathway in certain species of archaea and bacteria. In some organisms the enzyme is bifunctional and also catalyses the activity of EC 1.2.1.103, [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
2. |
Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630–21643. [DOI] [PMID: 27566549] |
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[EC 1.2.1.106 created 2021] |
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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) |
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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, PDB, 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] |
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[EC 1.4.1.18 created 1989, modified 2006, modified 2011] |
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EC |
1.4.3.20 |
Accepted name: |
L-lysine 6-oxidase |
Reaction: |
L-lysine + O2 + H2O = (S)-2-amino-6-oxohexanoate + H2O2 + NH3 |
Glossary: |
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
L-lysine-ε-oxidase; Lod; LodA; marinocine |
Systematic name: |
L-lysine:oxygen 6-oxidoreductase (deaminating) |
Comments: |
Differs from EC 1.4.3.13, protein-lysine 6-oxidase, by using free L-lysine rather than the protein-bound form. N2-Acetyl-L-lysine is also a substrate, but N6-acetyl-L-lysine, which has an acetyl group at position 6, is not a substrate. Also acts on L-ornithine, D-lysine and 4-hydroxy-L-lysine, but more slowly. The amines cadaverine and putrescine are not substrates [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1116448-48-6 |
References: |
1. |
Lucas-Elío, P., Gómez, D., Solano, F. and Sanchez-Amat, A. The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. J. Bacteriol. 188 (2006) 2493–2501. [DOI] [PMID: 16547036] |
2. |
Gómez, D., Lucas-Elío, P., Sanchez-Amat, A. and Solano, F. A novel type of lysine oxidase: L-lysine-ε-oxidase. Biochim. Biophys. Acta 1764 (2006) 1577–1585. [DOI] [PMID: 17030025] |
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[EC 1.4.3.20 created 2006, modified 2011] |
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EC |
1.5.1.9 |
Accepted name: |
saccharopine dehydrogenase (NAD+, L-glutamate-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH + H+ |
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Glossary: |
saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, glutamate-forming); saccharopin dehydrogenase; NAD+ oxidoreductase (L-2-aminoadipic-δ-semialdehyde and glutamate forming); aminoadipic semialdehyde synthase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-glutamate-forming) |
Comments: |
The activities of this enzyme along with EC 1.5.1.8, saccharopine dehydrogenase (NADP+, L-lysine-forming), occur on a single protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-26-1 |
References: |
1. |
Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62–69. [DOI] [PMID: 4385118] |
2. |
Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643–11646. [PMID: 6434529] |
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[EC 1.5.1.9 created 1972, modified 2011] |
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EC |
1.5.1.10 |
Accepted name: |
saccharopine dehydrogenase (NADP+, L-glutamate-forming) |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH + H+ |
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Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming) dehydrogenase; aminoadipic semialdehyde-glutamic reductase; aminoadipate semialdehyde-glutamate reductase; aminoadipic semialdehyde-glutamate reductase; ε-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming); saccharopine reductase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) |
Systematic name: |
N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-55-0 |
References: |
1. |
Jones, E.E. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase. J. Biol. Chem. 241 (1966) 3430–3434. [PMID: 4380448] |
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[EC 1.5.1.10 created 1972, modified 2011] |
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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] |
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[EC 1.5.3.7 created 1986, modified 2011] |
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EC |
1.5.3.18 |
Accepted name: |
L-saccharopine oxidase |
Reaction: |
N6-(L-1,3-dicarboxypropyl)-L-lysine + H2O + O2 = (S)-2-amino-6-oxohexanoate + L-glutamate + H2O2 |
Glossary: |
L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
FAP2 |
Systematic name: |
L-saccharopine:oxygen oxidoreductase (L-glutamate-forming) |
Comments: |
The enzyme is involved in pipecolic acid biosynthesis. A flavoprotein (FAD). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yoshida, N., Akazawa, S., Katsuragi, T. and Tani, Y. Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe. J. Biosci. Bioeng. 97 (2004) 278–280. [DOI] [PMID: 16233628] |
2. |
Wickwire, B.M., Wagner, C. and Broquist, H.P. Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis. J. Biol. Chem. 265 (1990) 14748–14753. [PMID: 2394693] |
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[EC 1.5.3.18 created 2011] |
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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] |
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[EC 1.5.99.3 created 1972, modified 1986, modified 2011] |
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EC |
2.6.1.36 |
Accepted name: |
L-lysine 6-transaminase |
Reaction: |
L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate |
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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] |
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[EC 2.6.1.36 created 1972, modified 2011] |
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EC |
2.6.1.39 |
Accepted name: |
2-aminoadipate transaminase |
Reaction: |
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate |
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Other name(s): |
α-aminoadipate aminotransferase; 2-aminoadipate aminotransferase; 2-aminoadipic aminotransferase; glutamic-ketoadipic transaminase; glutamate-α-ketoadipate transaminase |
Systematic name: |
L-2-aminoadipate:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9033-00-5 |
References: |
1. |
Matsuda, M. and Ogur, M. Separation and specificity of the yeast glutamate-α-ketoadipate transaminase. J. Biol. Chem. 244 (1969) 3352–3358. [PMID: 5792664] |
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[EC 2.6.1.39 created 1972] |
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EC |
2.6.1.71 |
Accepted name: |
lysine—pyruvate 6-transaminase |
Reaction: |
L-lysine + pyruvate = (S)-2-amino-6-oxohexanoate + L-alanine |
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Glossary: |
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
lysine-pyruvate aminotransferase; Lys-AT |
Systematic name: |
L-lysine:pyruvate aminotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 114189-79-6 |
References: |
1. |
Schmidt, H., Bode, R. and Birnbaum, D. A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii. FEMS Microbiol. Lett. 49 (1988) 203–206. |
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[EC 2.6.1.71 created 1990, modified 2011] |
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EC |
2.6.1.105 |
Accepted name: |
lysine—8-amino-7-oxononanoate transaminase |
Reaction: |
L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate |
Glossary: |
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
DAPA aminotransferase (ambiguous); bioA (gene name) (ambiguous); bioK (gene name) |
Systematic name: |
L-lysine:8-amino-7-oxononanoate aminotransferase |
Comments: |
A pyridoxal 5′-phosphate enzyme [2]. Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine—8-amino-7-oxononanoate transaminase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Van Arsdell, S.W., Perkins, J.B., Yocum, R.R., Luan, L., Howitt, C.L., Chatterjee, N.P. and Pero, J.G. Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction. Biotechnol. Bioeng. 91 (2005) 75–83. [DOI] [PMID: 15880481] |
2. |
Dey, S., Lane, J.M., Lee, R.E., Rubin, E.J. and Sacchettini, J.C. Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase. Biochemistry 49 (2010) 6746–6760. [DOI] [PMID: 20565114] |
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[EC 2.6.1.105 created 2014] |
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EC |
2.7.2.17 |
Accepted name: |
[amino-group carrier protein]-L-2-aminoadipate 6-kinase |
Reaction: |
ATP + an [amino-group carrier protein]-C-terminal-[N-(1,4-dicarboxybutyl)-L-glutamine] = ADP + an [amino-group carrier protein]-C-terminal-{N-[1-carboxy-5-oxo-5-(phosphooxy)pentyl]-L-glutamine} |
Other name(s): |
lysZ (gene name); [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine 5-O-kinase; [amino group carrier protein]-L-2-aminoadipate 6-kinase |
Systematic name: |
[amino-group carrier protein]-C-terminal-[N-(1,4-dicarboxybutyl)-L-glutamine] 5-O-kinase |
Comments: |
The enzyme participates in an L-lysine biosynthetic pathway in certain species of bacteria and archaea. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T. and Yamane, H. A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res. 9 (1999) 1175–1183. [PMID: 10613839] |
2. |
Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673–679. [DOI] [PMID: 19620981] |
3. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
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[EC 2.7.2.17 created 2020] |
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EC |
2.7.2.19 |
Accepted name: |
[amino-group carrier protein]-L-glutamate 6-kinase |
Reaction: |
ATP + an [amino-group carrier protein]-C-terminal-γ-(L-glutamyl)-L-glutamate = ADP + an [amino-group carrier protein]-C-terminal-γ-(5-phospho-L-glutamyl)-L-glutamate |
Other name(s): |
lysZ (gene name) |
Systematic name: |
[amino-group carrier protein]-C-terminal-γ-(L-glutamyl)-L-glutamine 5-O-kinase |
Comments: |
The enzyme participates in an L-arginine biosynthetic pathway in certain species of archaea. In some organisms the enzyme also catalyses the activity of EC 2.7.2.17, [amino-group carrier protein]-L-2-aminoadipate 6-kinase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
2. |
Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630–21643. [DOI] [PMID: 27566549] |
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[EC 2.7.2.19 created 2022] |
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EC |
6.3.2.43 |
Accepted name: |
[amino-group carrier protein]—L-2-aminoadipate ligase |
Reaction: |
ATP + an [amino-group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino-group carrier protein]-C-terminal-[N-(1,4-dicarboxybutyl)-L-glutamine] |
Other name(s): |
α-aminoadipate-lysW ligase; lysX (gene name); LysX (ambiguous); AAA—LysW ligase; [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming); [lysine-biosynthesis-protein LysW]—L-2-aminoadipate ligase |
Systematic name: |
[amino-group carrier protein]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming) |
Comments: |
The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW. This reaction is part of the lysine biosynthesis pathway in these organisms. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Vassylyeva, M.N., Sakai, H., Matsuura, T., Sekine, S., Nishiyama, M., Terada, T., Shirouzu, M., Kuramitsu, S., Vassylyev, D.G. and Yokoyama, S. Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 1651–1652. [PMID: 12925802] |
2. |
Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673–679. [DOI] [PMID: 19620981] |
3. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
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[EC 6.3.2.43 created 2014, modified 2019] |
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EC |
6.3.2.60 |
Accepted name: |
glutamate—[amino group carrier protein] ligase |
Reaction: |
ATP + L-glutamate + an [amino-group carrier protein]-C-terminal-L-glutamate = ADP + phosphate + an [amino-group carrier protein]-C-terminal-γ-(L-glutamyl)-L-glutamate |
Other name(s): |
argX (gene name) |
Systematic name: |
L-glutamate:an [amino-group carrier protein]-C-terminal-L-glutamate ligase (ADP-forming) |
Comments: |
The enzyme, originally characterized from the archaeon Sulfolobus acidocaldarius, is involved in L-arginine biosynthesis. The enzyme from the archaeon Thermococcus kodakarensis is bifunctional and also catalyses the activity of EC 6.3.2.43, [amino-group carrier protein]—L-2-aminoadipate ligase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
2. |
Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630–21643. [DOI] [PMID: 27566549] |
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[EC 6.3.2.60 created 2021] |
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