Ureohydrolase

The ureohydrolase superfamily includes arginase (EC 3.5.3.1), agmatinase (EC 3.5.3.11), formiminoglutamase (EC 3.5.3.8) and proclavaminate amidinohydrolase (EC 3.5.3.22).[2] These enzymes share a 3-layer alpha-beta-alpha structure,[2][3][4] and play important roles in arginine/agmatine metabolism, the urea cycle, histidine degradation, and other pathways.

Ureohydrolase
Identifiers
Symbol	Ureohydrolase
Pfam	PF00491
InterPro	IPR006035
PROSITE	PDOC00135
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB PDB: 1cev​ PDB: 1d3v​ PDB: 1gq6​ PDB: 1gq7​ PDB: 1hq5​ PDB: 1hqf​ PDB: 1hqg​ PDB: 1hqh​ PDB: 1hqx​ PDB: 1p8m​

A ureohydrolase is a type of hydrolase enzyme.[1]

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.[5] 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.[6]

Formiminoglutamase catalyses the fourth step in histidine degradation, acting to hydrolyse N-formimidoyl-L-glutamate to L-glutamate and formamide.

Proclavaminate amidinohydrolase is involved in clavulanic acid biosynthesis. Clavulanic acid acts as an inhibitor of a wide range of beta-lactamase enzymes that are used by various microorganisms to resist beta-lactam antibiotics. As a result, this enzyme improves the effectiveness of beta-lactamase antibiotics.[4][7]

References

1. Ureohydrolases at the US National Library of Medicine Medical Subject Headings (MeSH)
2. Lee J, Suh SW, Kim KH, Kim D, Yoon HJ, Kwon AR, Ahn HJ, Ha JY, Lee HH (2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): 50505–13. doi:10.1074/jbc.M409246200. PMID 15355972.
3. Christianson DW, Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F (2005). "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response". Proc. Natl. Acad. Sci. U.S.A. 102 (37): 13058–13063. doi:10.1073/pnas.0504027102. PMC 1201588. PMID 16141327.
4. Clifton IJ, Elkins JM, Hernandez H (2002). "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis". Biochem. J. 366 (Pt 2): 423. doi:10.1042/BJ20020125. PMC 1222790. PMID 12020346.
5. Baker BS, Tata JR, Xu Q (1993). "Developmental and hormonal regulation of the Xenopus liver-type arginase gene". Eur. J. Biochem. 211 (3): 891–898. doi:10.1111/j.1432-1033.1993.tb17622.x. PMID 7916684.
6. Ahn HJ, Kim KH, Lee J, et al. (November 2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): 50505–13. doi:10.1074/jbc.M409246200. PMID 15355972.
7. "IPR006035 Ureohydrolase". Retrieved 2009-02-17.

This article incorporates text from the public domain Pfam and InterPro: IPR006035