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Your query returned 11 entries. Printable version

1.1.1.259

Accepted name:

3-hydroxypimeloyl-CoA dehydrogenase

Reaction:

3-hydroxypimeloyl-CoA + NAD⁺ = 3-oxopimeloyl-CoA + NADH + H⁺

Glossary:

pimelic acid = heptanedioic acid

Systematic name:

3-hydroxypimeloyl-CoA:NAD⁺ oxidoreductase

Comments:

Involved in the anaerobic pathway of benzoate degradation in bacteria.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 1187536-27-1

References:

1.	Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301–309. [DOI] [PMID: 8990279]

[EC 1.1.1.259 created 2000]

1.3.1.26

Transferred entry:

dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase.

[EC 1.3.1.26 created 1976, modified 2011, deleted 2013]

1.3.1.62

Accepted name:

pimeloyl-CoA dehydrogenase

Reaction:

pimeloyl-CoA + NAD⁺ = 6-carboxyhex-2-enoyl-CoA + NADH + H⁺

Glossary:

pimelic acid = heptanedioic acid

Systematic name:

pimeloyl-CoA:NAD⁺ oxidoreductase

Comments:

Involved in the benzoate degradation (anaerobic) pathway in bacteria.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 276682-23-6

References:

1.	Gallus, C. and Schink, B. Anaerobic degradation of pimelate by newly isolated denitrifying bacteria. Microbiology 140 (1994) 409–416. [DOI] [PMID: 8180704]

[EC 1.3.1.62 created 2000]

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⁺

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]

[EC 1.17.1.8 created 1976 as EC 1.3.1.26, transferred 2013 to EC 1.17.1.8, modified 2020]

3.4.19.11

Accepted name:

γ-D-glutamyl-meso-diaminopimelate peptidase

Reaction:

Hydrolysis of γ-D-glutamyl bonds to the L-terminus (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-γ-D-Glu)-meso-A2pm and 7-(L-Ala-γ-D-Glu)-7-(D-Ala)-meso-A2pm. It is required that the D-terminal amino and carboxy groups of meso-A2pm are unsubstituted

Other name(s):

endopeptidase I; γ-D-glutamyldiaminopimelate endopeptidase; γ-D-glutamyl-L-meso-diaminopimelate peptidoglycan hydrolase; γ-glutamyl-L-meso-diaminopimelyl endopeptidase; γ-D-glutamyl-meso-diaminopimelate endopeptidase; γ-D-glutamyl-meso-diaminopimelic peptidoglycan hydrolase; γ-D-glutamyl-meso-diaminopimelic endopeptidase; γ-D-glutamyl-meso-D-aminopimelic endopeptidase

Comments:

A 45-kDa metallopeptidase from Bacillus sphaericus, the substrates being components of the bacterial spore wall. A member of peptidase family M14 (carboxypeptidase A family). Endopeptidase II has similar activity, but differs in cellular location, molecular mass and catalytic mechanism [3]

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 62572-28-5

References:

1.	Arminjon, F., Guinand, M., Vacheron, M.-J. and Michel, G. Specificity profiles of the membrane-bound γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase and LD-carboxypeptidase from Bacillus sphaericus 9602. Eur. J. Biochem. 73 (1977) 557–565. [DOI] [PMID: 849747]
2.	Garnier, M., Vacheron, M.-J., Guinard, M. and Michel, G. Purification and partial characterization of the extracellular γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase I, from Bacillus sphaericus NCTC 9602. Eur. J. Biochem. 148 (1985) 539–543. [DOI] [PMID: 3922755]
3.	Hourdou, M.-L., Guinand, M., Vacheron, M.-J., Michel, G., Denoroy, L., Duez, C., Englebert, S., Joris, B., Weber, G. and Ghuysen, J.-M. Characterization of the sporulation-related γ-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 as a member of the metallo(zinc) carboxypeptidase A family. Modular design of the protein. Biochem. J. 292 (1993) 563–570. [PMID: 8503890]

[EC 3.4.19.11 created 1996]

3.5.1.18

Accepted name:

succinyl-diaminopimelate desuccinylase

Reaction:

N-succinyl-LL-2,6-diaminoheptanedioate + H₂O = succinate + LL-2,6-diaminoheptanedioate

Other name(s):

N-succinyl-L-α,ε-diaminopimelic acid deacylase

Systematic name:

N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-94-6

References:

1.	Kindler, S.H. and Gilvarg, C. N-Succinyl-L-2,6-diaminopimelic acid deacylase. J. Biol. Chem. 235 (1960) 3532–3535. [PMID: 13756049]

[EC 3.5.1.18 created 1965]

3.5.1.47

Accepted name:

N-acetyldiaminopimelate deacetylase

Reaction:

N-acetyl-LL-2,6-diaminoheptanedioate + H₂O = acetate + LL-2,6-diaminoheptanedioate

Other name(s):

N-acetyl-L-diaminopimelic acid deacylase; N-acetyl-LL-diaminopimelate deacylase; 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase

Systematic name:

N⁶-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99193-93-8

References:

1.	Bartlett, A.T.M. and White, P.J. Species of Bacillus that make a vegetative peptidoglycan containing lysine lack diaminopimelate epimerase but have diaminopimelate dehydrogenase. J. Gen. Microbiol. 131 (1985) 2145–2152.
2.	Saleh, F. and White, P.J. Metabolism of DD-2,6-diaminopimelic acid by a diaminopimelate-requiring mutant of Bacillus megaterium. J. Gen. Microbiol. 115 (1979) 95–100.
3.	Sundharadas, G. and Gilvarg, C. Biosynthesis of α,ε-diaminopimelic acid in Bacillus megaterium. J. Biol. Chem. 242 (1967) 3983–3984. [PMID: 4962540]

[EC 3.5.1.47 created 1984 (EC 3.1.1.62 created 1989, incorporated 1992)]

4.1.1.20

Accepted name:

diaminopimelate decarboxylase

Reaction:

meso-2,6-diaminoheptanedioate = L-lysine + CO₂

Other name(s):

diaminopimelic acid decarboxylase; meso-diaminopimelate decarboxylase; DAP-decarboxylase; meso-2,6-diaminoheptanedioate carboxy-lyase

Systematic name:

meso-2,6-diaminoheptanedioate carboxy-lyase (L-lysine-forming)

Comments:

A pyridoxal-phosphate protein.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-75-3

References:

1.	Denman, R.F., Hoare, D.S. and Work, E. Diaminopimelic acid decarboxylase in pyridoxin-deficient Escherichia coli. Biochim. Biophys. Acta 16 (1955) 442–443. [DOI] [PMID: 14378182]

[EC 4.1.1.20 created 1961]

5.1.1.7

Accepted name:

diaminopimelate epimerase

Reaction:

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

Systematic name:

LL-2,6-diaminoheptanedioate 2-epimerase

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-22-0

References:

1.	Antia, M., Hoare, D.S. and Work, W. The stereoisomers of αε-diaminopimelic acid. 3. Properties and distribution of diaminopimelic acid racemase, an enzyme causing interconversion of the LL and meso isomers. Biochem. J. 65 (1957) 448–459. [PMID: 13412646]

[EC 5.1.1.7 created 1961]

6.2.1.14

Accepted name:

6-carboxyhexanoate—CoA ligase

Reaction:

ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate + 6-carboxyhexanoyl-CoA

Other name(s):

6-carboxyhexanoyl-CoA synthetase; pimelyl-CoA synthetase

Systematic name:

6-carboxyhexanoate:CoA ligase (AMP-forming)

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55467-50-0

References:

1.	Izumi, Y., Morita, H., Sato, K., Tani, Y. and Ogata, K. Synthesis of biotin-vitamers from pimelic acid and coenzyme A by cell-free extracts of various bacteria. Biochim. Biophys. Acta 264 (1972) 210–213. [DOI] [PMID: 4623286]
2.	Izumi, Y., Morita, H., Tani, Y. and Ogata, K. The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms. Agric. Biol. Chem. 38 (1974) 2257–2262.

[EC 6.2.1.14 created 1983]

7.4.2.12

Accepted name:

ABC-type cystine transporter

Reaction:

(1) ATP + H₂O + L-cystine-[cystine-binding protein]_{[side 1]} = ADP + phosphate + L-cystine_{[side 2]} + [cystine-binding protein]_{[side 1]}
(2) ATP + H₂O + D-cystine-[cystine-binding protein]_{[side 1]} = ADP + phosphate + D-cystine_{[side 2]} + [cystine-binding protein]_{[side 1]}

Other name(s):

cystine transporting ATPase; cystine ABC transporter

Systematic name:

ATP phosphohydrolase (ABC-type, cystine-importing)

Comments:

ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity import of trace cystine. The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Berger, E.A. and Heppel, L.A. A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J. Biol. Chem. 247 (1972) 7684–7694. [PMID: 4564569]
2.	Chonoles Imlay, K.R., Korshunov, S. and Imlay, J.A. Physiological roles and adverse effects of the two cystine importers of Escherichia coli. J. Bacteriol. 197 (2015) 3629–3644. [PMID: 26350134]

[EC 7.4.2.12 created 2019]