EC
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1.3.1.26
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Transferred entry: | dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase.
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[EC 1.3.1.26 created 1976, modified 2011, deleted 2013] |
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EC |
1.17.1.8 |
Accepted name: |
4-hydroxy-tetrahydrodipicolinate reductase |
Reaction: |
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+ |
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For diagram of lysine biosynthesis (early stages), click here |
Glossary: |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate = (2S)-2,3,4,5-tetrahydrodipicolinate |
Other name(s): |
dihydrodipicolinate reductase (incorrect); dihydrodipicolinic acid reductase (incorrect); 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase (incorrect); dapB (gene name) |
Systematic name: |
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+ 4-oxidoreductase |
Comments: |
The substrate of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1], and the enzyme was classified accordingly as EC 1.3.1.26, dihydrodipicolinate reductase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual substrate of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate, and that its activity includes a dehydration step [2], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate reductase. However, the identity of the substrate is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Farkas, W. and Gilvarg, C. The reduction step in diaminopimelic acid biosynthesis. J. Biol. Chem. 240 (1965) 4717–4722. [PMID: 4378965] |
2. |
Devenish, S.R., Blunt, J.W. and Gerrard, J.A. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J. Med. Chem. 53 (2010) 4808–4812. [DOI] [PMID: 20503968] |
3. |
Karsten, W.E., Nimmo, S.A., Liu, J. and Chooback, L. Identification of 2,3-dihydrodipicolinate as the product of the dihydrodipicolinate synthase reaction from Escherichia coli. Arch. Biochem. Biophys. 653 (2018) 50–62. [PMID: 29944868] |
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[EC 1.17.1.8 created 1976 as EC 1.3.1.26, transferred 2013 to EC 1.17.1.8, modified 2020] |
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EC |
2.3.1.89 |
Accepted name: |
tetrahydrodipicolinate N-acetyltransferase |
Reaction: |
acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + L-2-acetamido-6-oxoheptanedioate |
Other name(s): |
tetrahydrodipicolinate acetylase; tetrahydrodipicolinate:acetyl-CoA acetyltransferase; acetyl-CoA:L-2,3,4,5-tetrahydrodipicolinate N2-acetyltransferase; acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate 2-N-acetyltransferase |
Systematic name: |
acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N2-acetyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-91-4 |
References: |
1. |
Chatterjee, S.P. and White, P.J. Activities and regulation of the enzymes of lysine biosynthesis in a lysine-excreting strain of Bacillus megaterium. J. Gen. Microbiol. 128 (1982) 1073–1081. |
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[EC 2.3.1.89 created 1986] |
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EC |
2.3.1.117 |
Accepted name: |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase |
Reaction: |
succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate |
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Glossary: |
dipicolinate = pyridine-2,6-dicarboxylate |
Other name(s): |
tetrahydropicolinate succinylase; tetrahydrodipicolinate N-succinyltransferase; tetrahydrodipicolinate succinyltransferase; succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase; succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase |
Systematic name: |
succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase |
Comments: |
Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 88086-34-4 |
References: |
1. |
Simms, S.A., Voige, W.H. and Gilvarg, C. Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli. J. Biol. Chem. 259 (1984) 2734–2741. [PMID: 6365916] |
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[EC 2.3.1.117 created 1989, modified 2001] |
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EC |
2.6.1.83 |
Accepted name: |
LL-diaminopimelate aminotransferase |
Reaction: |
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O |
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For diagram of lysine biosynthesis (later stages), click here |
Glossary: |
LL-diaminopimelate = LL-2,6-diaminoheptanedioate
tetrahydrodipicolinate = tetrahydropyridine-2,6-dicarboxylate |
Other name(s): |
LL-diaminopimelate transaminase; LL-DAP aminotransferase; LL-DAP-AT |
Systematic name: |
LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate enzyme. In vivo, the reaction occurs in the opposite direction to that shown above. This is one of the final steps in the lysine-biosynthesis pathway of plants (ranging from mosses to flowering plants). meso-Diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates. 2-Oxoglutarate cannot be replaced by oxaloacetate or pyruvate. It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 949001-34-7 |
References: |
1. |
Hudson, A.O., Singh, B.K., Leustek, T. and Gilvarg, C. An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants. Plant Physiol. 140 (2006) 292–301. [DOI] [PMID: 16361515] |
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[EC 2.6.1.83 created 2006] |
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EC
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4.2.1.52
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Transferred entry: | dihydrodipicolinate synthase. Now EC 4.3.3.7, 4-hydroxy-2,3,4,5-tetrahydrodipicolinate synthase.
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[EC 4.2.1.52 created 1972, deleted 2012] |
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EC |
4.3.3.7 |
Accepted name: |
4-hydroxy-tetrahydrodipicolinate synthase |
Reaction: |
pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O |
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For diagram of lysine biosynthesis (early stages), click here |
Glossary: |
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate |
Other name(s): |
dihydrodipicolinate synthase (incorrect); dihydropicolinate synthetase (incorrect); dihydrodipicolinic acid synthase (incorrect); L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing); dapA (gene name). |
Systematic name: |
L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming] |
Comments: |
The reaction can be divided into three consecutive steps: Schiff base formation with pyruvate, the addition of L-aspartate-semialdehyde, and finally transimination leading to cyclization with simultaneous dissociation of the product. The product of the enzyme was initially thought to be (S)-2,3-dihydrodipicolinate [1,2], and the enzyme was classified accordingly as EC 4.2.1.52, dihydrodipicolinate synthase. Later studies of the enzyme from the bacterium Escherichia coli have suggested that the actual product of the enzyme is (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate [3], and thus the enzyme has been reclassified as 4-hydroxy-tetrahydrodipicolinate synthase. However, the identity of the product is still controversial, as more recently it has been suggested that it may be (S)-2,3-dihydrodipicolinate after all [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yugari, Y. and Gilvarg, C. The condensation step in diaminopimelate synthesis. J. Biol. Chem. 240 (1965) 4710–4716. [PMID: 5321309] |
2. |
Blickling, S., Renner, C., Laber, B., Pohlenz, H.D., Holak, T.A. and Huber, R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36 (1997) 24–33. [DOI] [PMID: 8993314] |
3. |
Devenish, S.R., Blunt, J.W. and Gerrard, J.A. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J. Med. Chem. 53 (2010) 4808–4812. [DOI] [PMID: 20503968] |
4. |
Soares da Costa, T.P., Muscroft-Taylor, A.C., Dobson, R.C., Devenish, S.R., Jameson, G.B. and Gerrard, J.A. How essential is the ’essential’ active-site lysine in dihydrodipicolinate synthase. Biochimie 92 (2010) 837–845. [DOI] [PMID: 20353808] |
5. |
Karsten, W.E., Nimmo, S.A., Liu, J. and Chooback, L. Identification of 2,3-dihydrodipicolinate as the product of the dihydrodipicolinate synthase reaction from Escherichia coli. Arch. Biochem. Biophys. 653 (2018) 50–62. [PMID: 29944868] |
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[EC 4.3.3.7 created 1972 as EC 4.2.1.52, transferred 2012 to EC 4.3.3.7, modified 2020] |
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