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In enzymology, a proclavaminate amidinohydrolase (EC 3.5.3.22) is an enzyme that catalyzes the chemical reaction

amidinoproclavaminate + H₂O ${\displaystyle \rightleftharpoons }$ proclavaminate + urea

Thus, the two substrates of this enzyme are amidinoproclavaminate and H₂O, whereas its two products are proclavaminate and urea.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is amidinoproclavaminate amidinohydrolase. Other names in common use include PAH, and proclavaminate amidino hydrolase. This enzyme participates in clavulanic acid biosynthesis.

References

• Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA (1991). "Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction". Biochemistry. 30 (8): 2281–92. doi:10.1021/bi00222a034. PMID 1998687.
• Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA (2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities". J. Am. Chem. Soc. 123 (30): 7388–98. doi:10.1021/ja004025+. PMID 11472170.
• Townsend CA (2002). "New reactions in clavulanic acid biosynthesis". Curr. Opin. Chem. Biol. 6 (5): 583–9. doi:10.1016/S1367-5931(02)00392-7. PMID 12413541.
• Wu TK, Busby RW, Houston TA, McIlwaine DB, Egan LA, Townsend CA (1995). "Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis". J. Bacteriol. 177 (13): 3714–20. PMC 177087. PMID 7601835.

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