Enzymology and gene technology of Streptomyces nucleotide 3'-pyrophosphokinase-2',3'-cyclic monophosphokinase (PPKase).

S. Ezaki, Shigeru Muta, S. Kuhara, J. Mukai

Research output: Contribution to journalArticlepeer-review

Abstract

Streptomyces extracellular nucleotide 3'-pyrophosphokinase-2',3'-cyclic monophosphokinase transfers 5'-beta,gamma-pyrophosphate group from ATP, some ATP derivatives and dATP to a variety of nucleot(s)ides at the 3'-OH site and synthesizes the respective 3'-pyrophosphoryl nucleotides. The enzyme also utilizes A-5'-pn (n = 3-5)-5'-N, transferring their adenosine 5'-pyrophosphoryl group and concomitantly eliminating the AMP moiety therefrom, leading to the synthesis of 2',3'-cyclic monophosphoryl nucleotides. The enzyme gene and its neighbouring up- and downstream sequences were analyzed. Streptomyces and enteric bacteria E. coli and Klebsiella pneumoniae transformants were constructed by incorporation of the pyrophosphokinase gene-recombined expression plasmids. Various effects of the treatments--intracellular synthesis of 3'-pyrophosphoryl nucleotides, retarded cellular growth, stimulated N2 fixation by K. pneumoniae and so on--were seen.

Original languageEnglish
Pages (from-to)131-132
Number of pages2
JournalNucleic acids symposium series
Issue number29
Publication statusPublished - Jan 1 1993

All Science Journal Classification (ASJC) codes

  • Medicine(all)

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