clavaminate synthase 2;
clavaminic acid synthase
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
(1) deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2 [RN:
(2) proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O [RN:
(3) dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O [RN:
Contains nonheme iron. Catalyses three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC
, proclavaminate amidinohydrolase. The three reactions are all catalysed at the same nonheme iron site.
EC 220.127.116.11 created 2003
ec00331 Clavulanic acid biosynthesis
ec01110 Biosynthesis of secondary metabolites
SCLF: BB341_07820 BB341_13950 » show all
Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA.
Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction.
Zhou, J., Gunsior, M., Bachmann, B.O., Townsend, C.A. and Solomon, E.I.
Substrate binding to the alpha-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation.
J Am Chem Soc 120:13539-13540 (1998)
Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.
Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA, Solomon EI.
Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities.
New reactions in clavulanic acid biosynthesis.
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