Pantetheine hydrolase

Short description: Class of enzymes

Structure of the pantetheinase vanin-1 from PDB: 4CYF​. Catalytic residues and sugars are shown in sticks, sugar-binding residues in lines.

Identifiers
EC number| 3.5.1.92
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
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PMC| articles
PubMed| articles
NCBI| proteins

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

(R)-pantetheine + H2O ⇌ (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.

## Further reading

* "Purification and properties of pantetheinase from horse kidney". Vitamins and Coenzymes Part D. Methods in Enzymology. 62. 1979. pp. 262–7. doi:10.1016/0076-6879(79)62227-9. ISBN 978-0-12-181962-0.
* "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. Bibcode: 1999FEBSL.461..149M.
* 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. Bibcode: 2000FEBSL.483..149P.
* "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). 2001. doi:10.1186/gb-2001-2-1-reviews0001. PMID 11380987.

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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
* Dihydroorotase

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

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Catalytically perfect enzyme
* Coenzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

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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