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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.5.1.54
667267
Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth
Appl. Environ. Microbiol.
72
2491-2495
2006
Enterobacter cloacae 99
16597948
3.5.1.54
733342
The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family
Biochemistry
52
690-700
2013
Granulibacter bethesdensis
23282241
3.5.1.54
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Granulibacter bethesdensis
27452902
3.5.1.54
753254
Theoretical investigation on binding process of allophanate to allophanate hydrolase
Chem. Res. Chin. Univ.
31
1023-1028
2015
Granulibacter bethesdensis
-
3.5.1.54
733342
The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family
Biochemistry
52
690-700
2013
Granulibacter bethesdensis ATCC BAA-1260
23282241
3.5.1.54
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Granulibacter bethesdensis ATCC BAA-1260
27452902
3.5.1.54
753254
Theoretical investigation on binding process of allophanate to allophanate hydrolase
Chem. Res. Chin. Univ.
31
1023-1028
2015
Granulibacter bethesdensis ATCC BAA-1260
-
3.5.1.54
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Granulibacter bethesdensis CGDN1H1
27452902
3.5.1.54
753254
Theoretical investigation on binding process of allophanate to allophanate hydrolase
Chem. Res. Chin. Univ.
31
1023-1028
2015
Granulibacter bethesdensis CGDNIH1
-
3.5.1.54
667259
Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism
Appl. Environ. Microbiol.
71
4437-4445
2005
Herbaspirillum huttiense
16085834
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