EC |
1.1.1.84 |
Accepted name: |
dimethylmalate dehydrogenase |
Reaction: |
(R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH |
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For diagram of pantothenate catabolism, click here |
Other name(s): |
β,β-dimethylmalate dehydrogenase |
Systematic name: |
(R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating) |
Comments: |
Requires K+ or NH4+ and Mn2+ or Co2+; also acts on (R)-malate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-21-8 |
References: |
1. |
Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409–416. [PMID: 4287371] |
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[EC 1.1.1.84 created 1972] |
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EC |
1.1.1.106 |
Accepted name: |
pantoate 4-dehydrogenase |
Reaction: |
(R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+ |
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For diagram of pantothenate catabolism, click here |
Glossary: |
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate |
Other name(s): |
pantoate dehydrogenase; pantothenase; D-pantoate:NAD+ 4-oxidoreductase |
Systematic name: |
(R)-pantoate:NAD+ 4-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-38-7 |
References: |
1. |
Goodhue, C.T. and Snell, E.E. The bacterial degradation of pantothenic acid. 3. Enzymatic formation of aldopantoic acid. Biochemistry 5 (1966) 403–408. [PMID: 4287370] |
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[EC 1.1.1.106 created 1972, modified 1976] |
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EC |
1.1.1.169 |
Accepted name: |
2-dehydropantoate 2-reductase |
Reaction: |
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+ |
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For diagram of the early stages of CoA biosynthesis, click here |
Glossary: |
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate |
Other name(s): |
2-oxopantoate reductase; 2-ketopantoate reductase; 2-ketopantoic acid reductase; ketopantoate reductase; ketopantoic acid reductase |
Systematic name: |
(R)-pantoate:NADP+ 2-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37211-74-8 |
References: |
1. |
King, H.L., Jr., Dyar, R.E. and Wilken, D.R. Ketopantoyl lactone and ketopantoic acid reductases. Characterization of the reactions and purification of two forms of ketopantoyl lactone reductase. J. Biol. Chem. 247 (1972) 4689–4695. [PMID: 4603075] |
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[EC 1.1.1.169 created 1976] |
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EC |
1.1.1.345 |
Accepted name: |
D-2-hydroxyacid dehydrogenase (NAD+) |
Reaction: |
an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+ |
Other name(s): |
LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous) |
Systematic name: |
(R)-2-hydroxycarboxylate:NAD+ oxidoreductase |
Comments: |
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640–660. [DOI] [PMID: 9126843] |
2. |
Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143–1150. [DOI] [PMID: 11120357] |
3. |
Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [DOI] [PMID: 16957230] |
4. |
Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [DOI] [PMID: 18391442] |
5. |
Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873–881. [DOI] [PMID: 19047348] |
6. |
Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [DOI] [PMID: 23954635] |
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[EC 1.1.1.345 created 2013] |
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EC |
1.2.1.33 |
Accepted name: |
(R)-dehydropantoate dehydrogenase |
Reaction: |
(R)-4-dehydropantoate + NAD+ + H2O = (R)-3,3-dimethylmalate + NADH + 2 H+ |
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For diagram of pantothenate catabolism, click here |
Other name(s): |
D-aldopantoate dehydrogenase; D-2-hydroxy-3,3-dimethyl-3-formylpropionate:diphosphopyridine nucleotide (DPN+) oxidoreductase |
Systematic name: |
(R)-4-dehydropantoate:NAD+ 4-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-96-7 |
References: |
1. |
Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409–416. [PMID: 4287371] |
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[EC 1.2.1.33 created 1972] |
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EC |
2.1.2.11 |
Accepted name: |
3-methyl-2-oxobutanoate hydroxymethyltransferase |
Reaction: |
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate |
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For diagram of the early stages of CoA biosynthesis, click here |
Other name(s): |
α-ketoisovalerate hydroxymethyltransferase; dehydropantoate hydroxymethyltransferase; ketopantoate hydroxymethyltransferase; oxopantoate hydroxymethyltransferase; 5,10-methylene tetrahydrofolate:α-ketoisovalerate hydroxymethyltransferase |
Systematic name: |
5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56093-17-5 |
References: |
1. |
Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. J. Biol. Chem. 251 (1976) 3786–3793. [PMID: 6463] |
2. |
Teller, J.H., Powers, S.G. and Snell, E.E. Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J. Biol. Chem. 251 (1976) 3780–3785. [PMID: 776976] |
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[EC 2.1.2.11 created 1982] |
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EC |
2.7.1.169 |
Accepted name: |
pantoate kinase |
Reaction: |
ATP + (R)-pantoate = ADP + (R)-4-phosphopantoate |
Other name(s): |
PoK; TK2141 protein |
Systematic name: |
ATP:(R)-pantoate 4-phosphotransferase |
Comments: |
The conversion of (R)-pantoate to (R)-4′-phosphopantothenate is part of the pathway leading to biosynthesis of 4′-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yokooji, Y., Tomita, H., Atomi, H. and Imanaka, T. Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea. J. Biol. Chem. 284 (2009) 28137–28145. [DOI] [PMID: 19666462] |
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[EC 2.7.1.169 created 2011] |
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EC |
3.5.1.22 |
Accepted name: |
pantothenase |
Reaction: |
(R)-pantothenate + H2O = (R)-pantoate + β-alanine |
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For diagram of pantothenate catabolism, click here |
Other name(s): |
pantothenate hydrolase; pantothenate amidohydrolase |
Systematic name: |
(R)-pantothenate amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9076-90-8 |
References: |
1. |
Nurmikko, V., Salo, E., Hakola, H., Makinen, K. and Snell, E.E. The bacterial degradation of pantothenic acid. II. Pantothenate hydrolase. Biochemistry 5 (1966) 399–402. [PMID: 5940928] |
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[EC 3.5.1.22 created 1972] |
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EC |
4.1.2.12 |
Accepted name: |
2-dehydropantoate aldolase |
Reaction: |
2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde |
Glossary: |
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate |
Other name(s): |
ketopantoaldolase; 2-dehydropantoate formaldehyde-lyase |
Systematic name: |
2-dehydropantoate formaldehyde-lyase (3-methyl-2-oxobutanoate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-51-5 |
References: |
1. |
McIntosh, E.N., Purko, M. and Wood, W.A. Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli. J. Biol. Chem. 228 (1957) 499–510. [PMID: 13475336] |
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[EC 4.1.2.12 created 1965, modified 2002] |
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EC |
6.3.2.1 |
Accepted name: |
pantoate—β-alanine ligase (AMP-forming) |
Reaction: |
ATP + (R)-pantoate + β-alanine = AMP + diphosphate + (R)-pantothenate |
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For diagram of coenzyme A biosynthesis (early stages), click here |
Glossary: |
(R)-pantoate = (2R)-2,4-dihydroxy-3,3-dimethylbutanoate
(R)-pantothenate = 3-[(2R)-2,4-dihydroxy-3,3-dimethylbutanamido]propanoate |
Other name(s): |
pantothenate synthetase; pantoate activating enzyme; pantoic-activating enzyme; D-pantoate:β-alanine ligase (AMP-forming); pantoate—β-alanine ligase (ambiguous) |
Systematic name: |
(R)-pantoate:β-alanine ligase (AMP-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-49-8 |
References: |
1. |
Ginoza, H.S. and Altenbern, R.A. The pantothenate-synthesizing enzyme cell-free extracts of Brucella abortus, strain 19. Arch. Biochem. Biophys. 56 (1955) 537–541. [DOI] [PMID: 14377603] |
2. |
Maas, W.K. Pantothenate studies. III. Description of the extracted pantothenate-synthesizing enzyme of Escherichia coli. J. Biol. Chem. 198 (1952) 23–32. [PMID: 12999714] |
3. |
Maas, W.K. Mechanism of the enzymatic synthesis of pantothenate from β-alanine and pantoate. Fed. Proc. 15 (1956) 305–306. |
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[EC 6.3.2.1 created 1961, modified 2014] |
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EC |
6.3.2.36 |
Accepted name: |
4-phosphopantoate—β-alanine ligase |
Reaction: |
ATP + (R)-4-phosphopantoate + β-alanine = AMP + diphosphate + (R)-4′-phosphopantothenate |
Other name(s): |
phosphopantothenate synthetase; TK1686 protein |
Systematic name: |
(R)-4-phosphopantoate:β-alanine ligase (AMP-forming) |
Comments: |
The conversion of (R)-pantoate to (R)-4′-phosphopantothenate is part of the pathway leading to biosynthesis of 4′-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphorylation (EC 6.3.2.1 [pantoate—β-alanine ligase] and EC 2.7.1.33 [pantothenate kinase], respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine. The two archaeal enzymes that catalyse this conversion are EC 2.7.1.169, pantoate kinase, and this enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Yokooji, Y., Tomita, H., Atomi, H. and Imanaka, T. Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea. J. Biol. Chem. 284 (2009) 28137–28145. [DOI] [PMID: 19666462] |
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[EC 6.3.2.36 created 2011] |
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EC |
6.3.2.44 |
Accepted name: |
pantoate—β-alanine ligase (ADP-forming) |
Reaction: |
ATP + (R)-pantoate + β-alanine = ADP + phosphate + (R)-pantothenate |
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For diagram of coenzyme A biosynthesis (early stages), click here |
Glossary: |
(R)-pantoate = (2R)-2,4-dihydroxy-3,3-dimethylbutanoate
(R)-pantothenate = 3-[(2R)-2,4-dihydroxy-3,3-dimethylbutanamido]propanoate |
Other name(s): |
pantothenate synthetase (ambiguous); pantoate—β-alanine ligase (ambiguous) |
Systematic name: |
(R)-pantoate:β-alanine ligase (ADP-forming) |
Comments: |
The enzyme, characterized from the archaeon Methanosarcina mazei, is involved in the biosynthesis of pantothenate. It is different from EC 6.3.2.1, the AMP-forming pantoate-β-alanine ligase found in bacteria and eukaryota. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ronconi, S., Jonczyk, R. and Genschel, U. A novel isoform of pantothenate synthetase in the Archaea. FEBS J. 275 (2008) 2754–2764. [DOI] [PMID: 18422645] |
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[EC 6.3.2.44 created 2014] |
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