Protein Family Models

Allophanate hydrolase (AH) converts allophanate to ammonium and carbon dioxide. The AH structure is composed of N- and C-terminal domains. These domains catalyze sequential reactions: the N-terminal domain converts allophanate to N-carboxycarbamate, whereas the C-terminal domain converts it to carbon dioxide and ammonium [2]. The C-terminal domain folds into alpha/beta structure in which some of the beta-strands form a barrel-like shape. Paper describing PDB structure 4gyr. [1]. 23282241. The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family. Lin Y, St Maurice M;. Biochemistry. 2013;52:690-700. Paper describing PDB structure 4iss. [2]. 23754281. Structure and function of allophanate hydrolase. Fan C, Li Z, Yin H, Xiang S;. J Biol Chem. 2013;288:21422-21432. Paper describing PDB structure 5c5z. [3]. 26249697. Crystal structure analysis of c4763, a uropathogenic Escherichia coli-specific protein. Kim H, Choi J, Kim D, Kim KK;. Acta Crystallogr F Struct Biol Commun. 2015;71:1042-1047. Paper describing PDB structure 5i8i. [4]. 29263142. Structure and function of urea amidolyase. Zhao J, Zhu L, Fan C, Wu Y, Xiang S;. Biosci Rep. 2018; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Allophanate hydrolase catalyzes the second reaction in an ATP-dependent two-step degradation of urea to ammonia and C02, following the action of the biotin-containing urea carboxylase. The yeast enzyme, a fusion of allophanate hydrolase to urea carboxylase, is designated urea amidolyase.

Gene:

atzF

Date:

2021-04-27

Date:

2020-10-26