Pantetheine hydrolase

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

Dupre S, Cavallini D (1979). "Purification and properties of pantetheinase from horse kidney". Methods Enzymol. Methods in Enzymology. 62: 262–7. doi:10.1016/0076-6879(79)62227-9. ISBN 978-0-12-181962-0. PMID 440106.
Dupre S, Chiaraluce R, Nardini M, Cannella C, Ricci G, Cavallini D (1984). "Continuous spectrophotometric assay of pantetheinase activity". Anal. Biochem. 142 (1): 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 (3): 149–52. 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.
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 (2–3): 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 (4): 296–306. doi:10.1007/s002510100327. PMID 11491533.
Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome Biol. 2 (1): REVIEWS0001. PMC 150437. PMID 11380987.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

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

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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