Pantetheine hydrolase

From Wikipedia, the free encyclopedia

In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction

(R)-pantetheine + H₂O $\rightleftharpoons$ (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.

[edit] References

IUBMB entry for 3.5.1.92
BRENDA references for 3.5.1.92 (Recommended.)
PubMed references for 3.5.1.92
PubMed Central references for 3.5.1.92
Google Scholar references for 3.5.1.92
Dupre S, Cavallini D (1979). "Purification and properties of pantetheinase from horse kidney". Methods. Enzymol. 62: 262–7. PMID 440106.
Dupre S, Chiaraluce R, Nardini M, Cannella C, Ricci G, Cavallini D (1984). "Continuous spectrophotometric assay of pantetheinase activity". Anal. Biochem. 142: 175–81. doi:10.1016/0003-2697(84)90534-7. PMID 6549111.
Maras B, Barra D, Dupre S, Pitari G (1999). "Is pantetheinase the actual identity of mouse and human vanin-1 proteins?". FEBS. Lett. 461: 149–52. doi:10.1016/S0014-5793(99)01439-8. PMID 10567687.
P (1996). "Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing". Immunity. 5: 391–405. doi:10.1016/S1074-7613(00)80496-3. PMID 8934567.
Maras B, Dupre S, Naquet P, Galland F (2000). "Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice". FEBS. Lett. 483: 149–54. doi:10.1016/S0014-5793(00)02110-4. PMID 11042271.
Granjeaud S, Mattei MG, Mungall AJ, Naquet P, Galland F (2001). "Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes". Immunogenetics. 53: 296–306. doi:10.1007/s002510100327. PMID 11491533.
Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome. Biol. 2: REVIEWS0001. PMID 11380987.