3.5.1.116: ureidoglycolate amidohydrolase
This is an abbreviated version!
For detailed information about ureidoglycolate amidohydrolase, go to the full flat file.
Word Map on EC 3.5.1.116
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3.5.1.116
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allantoin
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allantoate
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purine
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ureide
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ammonia
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glyoxylate
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allantoicase
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legumes
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aminohydrolase
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allophanate
- 3.5.1.116
- allantoin
- allantoate
- purine
-
ureide
- ammonia
- glyoxylate
- allantoicase
-
legumes
-
aminohydrolase
- allophanate
Reaction
Synonyms
(S)-ureidoglycine aminohydrolase, (S)-ureidoglycolate amidohydrolase, allA, amidase, ureidoglycolate, AtUAH, EC 3.5.3.19, OsUAH, UAH, UGDA, UGLYAH, ureidoglycolate amidohydrolase, ureidoglycolate hydrolase
ECTree
3.5.1.116 ureidoglycolate amidohydrolaseAdvanced search results
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results (Engineering
Engineering on EC 3.5.1.116 - ureidoglycolate amidohydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E183A
H290Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H424N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q257N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y423F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
E183A
site-directed mutagenesis, inactive mutant, crystal structure analysis
additional information
conferring an allantoate amidinohydrolase-like activity on the enzyme by redesigning the size of the (S)-ureidoglycolate amidohydrolase active site and modifying the substrate specifiicty is not successfull by simply relieving the possible steric hindrance of Tyr423 to the incoming pro-S ureido group in allantoate.The AtUAH Y423G mutant is inactive with allantoate. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
additional information
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conferring an allantoate amidinohydrolase-like activity on the enzyme by redesigning the size of the (S)-ureidoglycolate amidohydrolase active site and modifying the substrate specifiicty is not successfull by simply relieving the possible steric hindrance of Tyr423 to the incoming pro-S ureido group in allantoate.The AtUAH Y423G mutant is inactive with allantoate. Substrate specificity in the (S)-ureidoglycolate amidohydrolase is a function of interactions more complex than those conferred by a single active-site residue
