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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
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
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
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
718475
The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase
Acta Crystallogr. Sect. D
67
105-111
2011
no activity in Thermus thermophilus
21245531
3.5.1.54
774125
Urease-negative uropathogen Kalamiella piersonii YU22 metabolizes urea by urea carboxylase and allophanate hydrolase enzyme system
Microbiol. Res.
263
127142
2022
Pantoea piersonii
35940107
3.5.1.54
774125
Urease-negative uropathogen Kalamiella piersonii YU22 metabolizes urea by urea carboxylase and allophanate hydrolase enzyme system
Microbiol. Res.
263
127142
2022
Pantoea piersonii YU22
35940107
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
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Saccharomyces cerevisiae
27452902
3.5.1.54
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Candida albicans
27452902
3.5.1.54
746393
The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent
Protein Sci.
25
1812-1824
2016
Pseudomonas syringae pv. tomato
27452902
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