Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase

Journal of Basic Microbiology
Martin JarlingHermann Pape

Abstract

The gene mak1FN coding for maltokinase from Actinoplanes missouriensis is located in a cluster similar to glycogen metabolism clusters identified in Streptomyces coelicolor. Sequence comparisons demonstrate that mak1-related genes coding for homologous proteins are present in many bacterial genomes including taxonomic distantly related groups such as Rhodospirillales or green sulfur bacteria. More than 50% of the aligned sequences are longer than the mak1 gene from A. missouriensis, and the N-terminal portion of these putative maltokinases exhibit high sequence homologies with trehalose synthases. A more detailed sequence comparison indicates a relationship of maltokinases to aminoglycoside phospho-transferases and protein kinases. Transformation of S. lividans with plasmid vectors containing either the mak1 gene from A. missouriensis or the pep2 gene from S. coelicolor resulted in recombinant strains, which produced measurable amounts of maltokinase activity. The proteins Pep2 and Mak1 were over expressed with Streptomyces lividans 66 as a heterologous host and further characterized. The possible physiological function of maltokinases is discussed.

Citations

Mar 23, 2010·Nature Chemical Biology·Rainer KalscheuerWilliam R Jacobs
May 29, 2010·BMC Biochemistry·Vítor MendesNuno Empadinhas
Mar 16, 2007·PLoS Biology·Natarajan KannanGerard Manning
Feb 15, 2013·Standards in Genomic Sciences·Hideki YamamuraMasayuki Hayakawa
Mar 5, 2016·MedChemComm·Sandeep Thanna, Steven J Sucheck
Jan 27, 2015·Scientific Reports·Joana FragaSandra Macedo-Ribeiro
Jan 12, 2020·Applied Microbiology and Biotechnology·Masayoshi Sakaguchi
Feb 11, 2016·Biochemical Society Transactions·Stephen Bornemann

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