Pantetheine Hydrolase

From Handwiki
Pantetheine hydrolase
Identifiers
EC number3.5.1.92
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. 




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Categories: [EC 3.5.1] [Enzymes of unknown structure]


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