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Results 1 - 6 of 6
EC Number
Amino acid exchange
Commentary
Reference
A46G
mutation in loop L1. Probability of being in open conformation is higher than that of wild-type, yielding an increased level of solvent exposure of the active site. The flavin fluorescence intensity is about 2fold higher than in wild-type. Loop L1 is important for substrate capture and catalysis
E87L
kcat/Km pH-profile of the E87L mutant indicates only a single unprotonated group is required for maximal activity with D-arginine. E87 is the unprotonated group on the enzyme that binds cationic substrates
H48F
residue H48 is not responsible for the observed pKa value
S45A
mutation in loop L1. Probability of being in open conformation is higher than that of wild-type, yielding an increased level of solvent exposure of the active site. The flavin fluorescence intensity is about 2fold higher than in wild-type. Loop L1 is important for substrate capture and catalysis
Y249F
steady-state kinetic parameters similar to those of the wild-type enzyme. Rate constants for flavin reduction (kred) with D-leucine are 3fold smaller than the wild-type value with similar pKa values for an unprotonated group of about 10.0. Cleavage of the substrate NH and CH bonds in the enzyme variant occurs in synchronous fashion, which can be reconciled with a hydride transfer mechanism
Y53F
steady-state kinetic parameters similar to those of the wild-type enzyme. Rate constants for flavin reduction (kred) with D-leucineare 3fold smaller than the wild-type value with similar pKa values for an unprotonated group of about 10.0. Cleavage of the substrate NH and CH bonds in the enzyme variant occurs in synchronous fashion, which can be reconciled with a hydride transfer mechanism
Results 1 - 6 of 6