| Pantetheine hydrolase |
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| Identifiers |
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| EC number | 3.5.1.92 |
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| Databases |
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| IntEnz | IntEnz view |
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| BRENDA | BRENDA entry |
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| ExPASy | NiceZyme view |
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| KEGG | KEGG entry |
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| MetaCyc | metabolic pathway |
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| PRIAM | profile |
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| PDB structures | RCSB PDB PDBe PDBsum |
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| Search |
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| PMC | articles |
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| PubMed | articles |
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| NCBI | proteins |
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In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction
- (R)-pantetheine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] (R)-pantothenate + 2-aminoethanethiol
Thus, the two substrates of this enzyme are (R)-pantetheine and H2O, whereas its two products are (R)-pantothenate and 2-aminoethanethiol.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (R)-pantetheine amidohydrolase. Other names in common use include pantetheinase, vanin, and vanin-1. This enzyme participates in pantothenate and coa biosynthesis.
References
- "Purification and properties of pantetheinase from horse kidney". Methods Enzymol.. Methods in Enzymology 62: 262–7. 1979. doi:10.1016/0076-6879(79)62227-9. ISBN 978-0-12-181962-0. PMID 440106.
- "Continuous spectrophotometric assay of pantetheinase activity". Anal. Biochem. 142 (1): 175–81. 1984. doi:10.1016/0003-2697(84)90534-7. PMID 6549111.
- "Is pantetheinase the actual identity of mouse and human vanin-1 proteins?". FEBS Lett. 461 (3): 149–52. 1999. doi:10.1016/S0014-5793(99)01439-8. PMID 10567687.
- P; Galland, F; Bazin, H; Zakharyev, VM; Imhof, BA; Naquet, P (1996). "Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing". Immunity 5 (5): 391–405. doi:10.1016/S1074-7613(00)80496-3. PMID 8934567.
- "Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice". FEBS Lett. 483 (2–3): 149–54. 2000. doi:10.1016/S0014-5793(00)02110-4. PMID 11042271.
- "Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes". Immunogenetics 53 (4): 296–306. 2001. doi:10.1007/s002510100327. PMID 11491533.
- "The nitrilase superfamily: classification, structure and function". Genome Biol. 2 (1): REVIEWS0001. 2001. doi:10.1186/gb-2001-2-1-reviews0001. PMID 11380987.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) |
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3.5.1: Linear amides / Amidohydrolases |
- Asparaginase
- Glutaminase
- Urease
- Biotinidase
- Aspartoacylase
- Ceramidase
- Aspartylglucosaminidase
- Fatty acid amide hydrolase
- Histone deacetylase
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3.5.2: Cyclic amides/ Amidohydrolases |
- Barbiturase
- Beta-lactamase
- Dihydroorotase
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3.5.3: Linear amidines/ Ureohydrolases |
- Arginase
- Agmatinase
- Protein-arginine deiminase
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3.5.4: Cyclic amidines/ Aminohydrolases |
- Guanine deaminase
- Adenosine deaminase
- AMP deaminase
- Inosine monophosphate synthase
- DCMP deaminase
- GTP cyclohydrolase I
- Cytidine deaminase
- AICDA
- Activation-induced cytidine deaminase
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3.5.5: Nitriles/ Aminohydrolases | |
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| 3.5.99: Other |
- Riboflavinase
- Thiaminase II
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Enzymes |
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
- Enzyme activator
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
- EC7 Translocases (list)
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 | Original source: https://en.wikipedia.org/wiki/Pantetheine hydrolase. Read more |