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Results 1 - 10 of 19 > >>
EC Number
Activating Compound
Commentary
Reference
Ferredoxin
methylviologen can replace ferredoxin
Ferredoxin
reactivation of inactive enzyme requires reduced ferredoxin, Fe2+-dithiol or Co2+-mercaptoethanol complexes can substitute for ferredoxin
more
conversion into the active form is carried out by an activating system containing a flavodoxin system and an activating enzyme (pyruvate format lyase-activase, EC 1.97.1.4)
NADPH
more effective for activation than NADPH, 0.02 mM NADPH activates over 80% inactive enzyme in cell-free extracts
oxamate
-
oxamate
obligatory component of the activation reaction
pyruvate
obligatory component of the activation reaction
pyruvate formate lyase activating enzyme
activates the enzyme by forming a glycine radical, cf. EC 1.97.1.4
pyruvate formate-lyase activating enzyme
PFL-AE, EC 1.97.1.4, is a radical S-adenosyl-L-methionine enzyme that utilizes an iron-sulfur cluster and S-adenosyl-L-methionine to activate pyruvate formate lyase (PFL) via pro-S hydrogen abstraction from Gly734. Usage of an S-adenosyl-L-methionine binding assay to accurately determine the equilibrium constants for S-adenosyl-L-methionine binding to enzyme PFL-AE alone and in complex with substrate PFL, activation of PFL in the presence of its substrate pyruvate or the analogue oxamate results in stoichiometric conversion of the [4Fe-4S]1+ cluster to the glycyl radical on PFL. 3.7fold less activation is achieved in the absence of these small molecules, demonstrating that pyruvate or oxamate are required for optimal activation. For the assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures. PFL activation studies, binding kinetics, overview
Results 1 - 10 of 19 > >>