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The Pur10 protein encoded in the gene cluster for puromycin biosynthesis of Streptomyces alboniger is an NAD‐dependent ATP dehydrogenase
Author(s) -
Rubio Miguel Angel,
Espinosa Juan Carlos,
Tercero José Antonio,
Jiménez Antonio
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01228-9
Subject(s) - puromycin , nad+ kinase , biochemistry , biosynthesis , gene cluster , escherichia coli , dehydrogenase , biology , streptomyces , recombinant dna , gene , protein biosynthesis , histidine , microbiology and biotechnology , chemistry , enzyme , bacteria , genetics
The pur10 gene of the puromycin ( pur ) cluster of Streptomyces alboniger is essential for the biosynthesis of this antibiotic. Highly purified Pur10 protein, obtained in Escherichia coli as a recombinant protein fused to a histidine tail, had an NAD‐dependent ATP dehydrogenase activity. The K m and V max values for ATP were 0.49 mM and 14.5 nmol/min and for NAD 0.53 mM and 15.2 nmol/min, respectively. The ATP‐derived product of the reaction apparently decomposed producing a triphosphorylated compound plus an adenine derivative. These and previous results suggested that Pur10 carries out the first step of the puromycin biosynthetic pathway, namely, conversion of ATP into 3′‐keto‐3′‐deoxyATP.