PMID: 8947483Nov 15, 1996Paper

New type of hexameric ornithine carbamoyltransferase with arginase activity in the cephamycin producers Streptomyces clavuligerus and Nocardia lactamdurans

The Biochemical Journal
J L de La FuenteP Liras

Abstract

The ornithine carbamoyltransferases (OTCases) from the beta-lactam-producing actinomycetes Streptomyces clavuligerus and Nocardia lactamdurans have been purified to near-homogeneity by delta-N-phosphonoacetylornithine-Sepharose 4B affinity chromatography. The S. clavuligerus and N. lactamdurans OTCases monomers had a molecular mass of 37 kDa. The native OTCases of S. clavuligerus, N. lactamdurans and Streptomyces coelicolor had molecular masses of 248, 251 and 247 kDa respectively, which correspond to a hexameric structure. The apparent K(m) values for ornithine and carbamoylphosphate of the S. clavuligerus enzyme were respectively 2.3 and 6.0 mM at pH 8.0. The enzyme showed a reverse activity on citrulline and used lysine and putrescine as substrates. The hexameric complex showed coupled arginase-OTCase activities and was able to convert arginine into citrulline in a carbamoylphosphate-dependent manner. The requirement for carbamoylphosphate might prevent the arginase-OTCase complex from carrying out a futile cycle of arginine biosynthesis and degradation.

Citations

Aug 15, 2015·International Journal of Molecular Sciences·Dashuang ShiMendel Tuchman
Mar 10, 2012·PloS One·Rosario Pérez-RedondoPaloma Liras
Nov 27, 2002·Molecular Phylogenetics and Evolution·Manuel ZúñigaFernando González-Candelas
Jul 19, 2018·Antibiotics·Daniela de Araújo Viana MarquesAna Lúcia Figueiredo Porto
May 23, 2006·The British Journal of Dermatology·V MadanJ T Lear

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