| pantothenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.22 | ||||||||
| CAS no. | 9076-90-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a pantothenase (EC 3.5.1.22) is an enzyme that catalyzes the chemical reaction
- (R)-pantothenate + H2O (R)-pantoate + beta-alanine
(R)-pantoate + beta-alanineThus, the two substrates of this enzyme are (R)-pantothenate and H2O, whereas its two products are (R)-pantoate and beta-alanine.
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)-pantothenate amidohydrolase. Other names in common use include pantothenate hydrolase, and pantothenate amidohydrolase. This enzyme participates in pantothenate and coa biosynthesis.
References
- Nurmikko V, Salo E, Hakola H, Makinen K, Snell EE (1966). "The bacterial degradation of pantothenic acid. II. Pantothenate hydrolase". Biochemistry. 5 (2): 399–402. doi:10.1021/bi00866a002. PMID 5940928.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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