EC |
1.1.1.358 |
Accepted name: |
2-dehydropantolactone reductase |
Reaction: |
(R)-pantolactone + NADP+ = 2-dehydropantolactone + NADPH + H+ |
Other name(s): |
2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase |
Systematic name: |
(R)-pantolactone:NADP+ oxidoreductase |
Comments: |
The enzyme participates in an alternative pathway for biosynthesis of (R)-pantothenate (vitamin B5). This entry covers enzymes whose stereo specificity for NADP+ is not known. cf. EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific) and EC 1.1.1.214, 2-dehydropantolactone reductase (Si-specific). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hata, H., Shimizu, S., Hattori, S. and Yamada, H. Ketopantoyl-lactone reductase from Candida parapsilosis: purification and characterization as a conjugated polyketone reductase. Biochim. Biophys. Acta 990 (1989) 175–181. [DOI] [PMID: 2644973] |
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[EC 1.1.1.358 created 2013] |
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EC |
2.7.1.33 |
Accepted name: |
pantothenate kinase |
Reaction: |
ATP + (R)-pantothenate = ADP + (R)-4′-phosphopantothenate |
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For diagram of the late stages of CoA biosynthesis, click here |
Other name(s): |
pantothenate kinase (phosphorylating); pantothenic acid kinase; ATP:pantothenate 4′-phosphotransferase; D-pantothenate kinase |
Systematic name: |
ATP:(R)-pantothenate 4′-phosphotransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9026-48-6 |
References: |
1. |
Abiko, Y., Ashida, S.-I. and Shimizu, M. Purification and properties of D-pantothenate kinase from rat liver. Biochim. Biophys. Acta 268 (1972) 364–372. [DOI] [PMID: 4337331] |
2. |
Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370–378. [PMID: 13630913] |
3. |
Pierpoint, W.S., Hughes, D.E., Baddiley, J. and Mathias, A.P. The phosphorylation of pantothenic acid by Lactobacillus arabinosus 17-5. Biochem. J. 61 (1955) 368–374. [PMID: 13269369] |
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[EC 2.7.1.33 created 1961] |
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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 |
3.5.1.92 |
Accepted name: |
pantetheine hydrolase |
Reaction: |
(R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol |
Other name(s): |
pantetheinase; vanin; vanin-1 |
Systematic name: |
(R)-pantetheine amidohydrolase |
Comments: |
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56093-18-6 |
References: |
1. |
Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262–267. [PMID: 440106] |
2. |
Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175–181. [DOI] [PMID: 6549111] |
3. |
Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149–152. [DOI] [PMID: 10567687] |
4. |
Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus
homing. Immunity 5 (1996) 391–405. [DOI] [PMID: 8934567] |
5. |
Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Duprè, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149–154. [DOI] [PMID: 11042271] |
6. |
Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode
isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296–306. [PMID: 11491533] |
7. |
Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.. [PMID: 11380987] |
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[EC 3.5.1.92 created 2006] |
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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 |
6.3.2.44 |
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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