The amino acid sequence of rat kidney 5-oxo-L-prolinase determined by cDNA cloning.

The Journal of Biological Chemistry
G J YeA Meister

Abstract

5-Oxoprolinase (EC 3.5.2) catalyzes a reaction in which the endergonic cleavage of 5-oxo-L-proline to form L-glutamate is coupled to the exergonic hydrolysis of ATP to ADP and inorganic phosphate. Highly purified preparations of the enzyme have been obtained from rat kidney and Pseudomonas putida. The rat kidney enzyme is composed of two strongly interacting, apparently identical subunits (Mr = 142,000), whereas that from P. putida is composed of two functionally different protein components that can readily be dissociated. Here we report the cloning of rat kidney 5-oxoprolinase with preliminary expression studies. cDNA clones encoding the enzyme were isolated by screening a lambdagt11 cDNA library beginning with a degenerate oligonucleotide probe based on peptide sequence data obtained from the purified enzyme. The whole cDNA clone was completed by amplifying its 5' end from a premade library of rat kidney Marathon-ReadyTM cDNAs using polymerase chain reaction methodology. The composite cDNA (4,016 bases) revealed an uninterrupted open reading frame encoding 1,288 amino acid residues (Mr = 137,759). The deduced amino acid sequence contains all four of the peptide sequences that were independently found in peptide fragments der...Continue Reading

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Citations

Mar 17, 1999·Journal of Biochemical and Biophysical Methods·P WeberS Wolf
Mar 3, 2004·Biological & Pharmaceutical Bulletin·Tohru WatanabeYasuteru Iijima
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Apr 19, 2003·FEMS Yeast Research·Michel J Penninckx
May 26, 2017·Antioxidants & Redox Signaling·Anand Kumar Bachhawat, Amandeep Kaur
Jun 1, 2018·Applied Microbiology and Biotechnology·Marleen OtzenDick B Janssen

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