Ureohydrolase domain superfamily
IPR023696
Definition
This entry represents hydrolases that cleave carbon-nitrogen bonds other than peptide bonds ([ec:3.5.-.-]). It includes mainly members of the ureohydrolase superfamily. It also represents the histone deacetylase family ([ec:3.5.1.98]) and other related hydrolases. The ureohydrolase superfamily includes arginase ([ec:3.5.3.1]), agmatinase ([ec:3.5.3.11]), formimidoylglutamase (also known as formiminoglutamase; [ec:3.5.3.8]) and proclavaminate amidinohydrolase ([ec:3.5.3.22]) PMID:15355972. These enzymes share a 3-layer α-β-α structure [[cite:PMID:15355972], [cite:PMID:16141327], [cite:PMID:12020346]], and play important roles in arginine/agmatine metabolism, the urea cycle, histidine degradation, and other pathways. Arginase, which catalyses the conversion of arginine to urea and ornithine, is one of the five members of the urea cycle enzymes that convert ammonia to urea as the principal product of nitrogen excretion PMID:7916684. There are several arginase isozymes that differ in catalytic, molecular and immunological properties. Deficiency in the liver isozyme leads to argininemia, which is usually associated with hyperammonemia. Agmatinase hydrolyses agmatine to putrescine, the precursor for the biosynthesis of higher polyamines, spermidine and spermine. In addition, agmatine may play an important regulatory role in mammals.
14 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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