Pantetheine hydrolase

Pantetheine hydrolase
Structure of the pantetheinase vanin-1 from PDB: 4CYF​. Catalytic residues and sugars are shown in sticks, sugar-binding residues in lines.
Identifiers
EC no.3.5.1.92
Databases
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Pantetheine hydrolase (EC 3.5.1.92) is an enzyme characterised from kidney that catalyzes the hydrolysis of one of the two amide bonds in pantetheine, giving pantothenic acid and cysteamine:

2D representation of the chemical structure of pantetheine.
pantetheine
 
H2O
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 
2D representation of the chemical structure of pantothenic acid .
pantothenic acid
+
 
2D representation of the chemical structure of cysteamine.
cysteamine

The enzyme is part of the catabolism of pantethine (vitamin B5) and one product, cysteamine, is an antioxidant. In humans, the enzyme is a vanin-1 protein. It has a role in inflammatory diseases like asthma.

This enzyme is a hydrolase, one 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.

References

  1. ↑ Dupre S, Cavallini D (1979). "Purification and properties of pantetheinase from horse kidney". Vitamins and Coenzymes Part D. Methods in Enzymology. Vol. 62. pp. 262–7. doi:10.1016/0076-6879(79)62227-9. ISBN 978-0-12-181962-0. PMID 440106.
  2. ↑ 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.
  3. ↑ 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. Bibcode:2000FEBSL.483..149P. doi:10.1016/S0014-5793(00)02110-4. PMID 11042271.
  4. ↑ 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. Bibcode:1999FEBSL.461..149M. doi:10.1016/S0014-5793(99)01439-8. PMID 10567687.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ Dai, Dianfeng; Zhang, Zhimin; Ma, Mo; et al. (2025). "Vanin-1-Activated Fluorescent Probe for Real-Time In Vivo Imaging of Inflammatory Responses Across Multiple Tissue Types". Analytical Chemistry. 97 (2): 1402–1409. doi:10.1021/acs.analchem.4c05982. PMID 39787461.
  8. ↑ Jiang, Yuhan; Guo, Ju; Wang, Yifan; et al. (2026). "From early-onset asthma to chronic obstructive pulmonary disease: Potential mediating proteins and therapeutic targets". Briefings in Bioinformatics. 27 (3) bbag209. doi:10.1093/bib/bbag209. PMC 13147455. PMID 42089751.
  9. ↑ Enzyme 3.5.1.92 at KEGG Pathway Database.
  10. ↑ Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function". Genome Biol. 2 (1) REVIEWS0001. doi:10.1186/gb-2001-2-1-reviews0001. PMC 150437. PMID 11380987.