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3.5.1.84: biuret amidohydrolase

This is an abbreviated version!
For detailed information about biuret amidohydrolase, go to the full flat file.

Word Map on EC 3.5.1.84

Reaction

Biuret
+
H2O
=
urea-1-carboxylate
 +
NH3

Synonyms

BiuH, biuret hydrolase, biuret-hydrolyzing enzyme, biuretase, hydrolase, biuret, trzE gene product

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.84 biuret amidohydrolase

Engineering

Engineering on EC 3.5.1.84 - biuret amidohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C175S
the mutant enzyme binds biuret but is non-catalytic. The structure of the inactive C175S mutant enzyme with substrate bound in the active site reveals that an active site cysteine (Cys175), aspartic acid (Asp36) and lysine (Lys142) form a catalytic triad, which is consistent with biochemical studies of enzyme variants
F41A
kcat/Km for buiret is 540fold lower than the wild-type value
F41L
kcat/Km for buiret is 713fold lower than the wild-type value
F41W
kcat/Km for buiret is 73fold lower than the wild-type value
F41Y
kcat/Km for buiret is 139fold lower than the wild-type value
K142A
kcat/Km for buiret is 297fold lower than the wild-type value
Q215A
kcat/Km for buiret is 419fold lower than the wild-type value
Q215E
kcat/Km for buiret is 1302fold lower than the wild-type value
Q215N
kcat/Km for buiret is 38fold lower than the wild-type value