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

  title={Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase},
  author={Martin Jarling and Thomas Cauvet and Matthias Grundmeier and Katharina Kuhnert and Hermann Pape},
  journal={Journal of Basic Microbiology},
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… Expand
Biochemical characterization of the maltokinase from Mycobacterium bovis BCG
The unknown role of maltokinases in mycobacterial metabolism and the lack of biochemical data led us to express the mak gene from M. bovis BCG for biochemical characterization, which is the first myc Cobacterial Mak to be characterized. Expand
Developmental delay in a Streptomyces venezuelae glgE null mutant is associated with the accumulation of α-maltose 1-phosphate
High levels ofα-maltose 1-phosphate are responsible for the developmental phenotype of the ΔglgE mutant, rather than the lack of α-glucan, and the GlgE pathway is necessary and sufficient for polymer biosynthesis. Expand
Glucan metabolism in Mycobacterium and Streptomyces
Streptomyces venezuelae was used to show for the first time that the GlgE pathway is responsible for glucan synthesis in vivo, as was predicted by the annotations in the genome. Expand
Three trehalose synthetic pathways in the acarbose-producing Actinoplanes sp. SN223/29 and evidence for the TreY role in biosynthesis of component C
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Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway
The structural characterization of the fourth enzyme of the pathway, mycobacterial maltokinase (Mak), is described, uncovering a eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases, which has a novel N-terminal domain topologically resembling the cystatin family of protease inhibitors. Expand
Complete genome sequence of the motile actinomycete Actinoplanes missouriensis 431T (= NBRC 102363T)
The features of A. missouriensis 431T are described, together with the complete genome sequence and annotation, and it is shown that members of Actinoplanes are prolific sources of novel antibiotics, enzymes, and other bioactive compounds. Expand
Comparative proteome analysis of Actinoplanes utahensis grown on various saccharides based on 2D-DIGE and MALDI-TOF/TOF-MS.
Comparative proteomes of Actinoplanes utahensis ZJB-03852 grown on various saccharides and fundamental data revealed fundamental data to elucidate the complexity of formation of acarbose analogues to treat Type II diabetes. Expand
Last Step in the Conversion of Trehalose to Glycogen
It is proposed that trehalose synthase, maltokinase, and GMPMT represent a new pathway of glycogen synthesis using tre Halose as the source of glucose. Expand
Trehalose During Two Stress Responses in Acanthamoeba: Differentiation Between Encystation and Pseudocyst Formation.
The data clearly demonstrate fundamental differences between encystation and pseudocyst formation at the level of cellular metabolism in the facultatively parasitic organism Acanthamoeba castellanii. Expand
Diverse and common features of trehalases and their contributions to microbial trehalose metabolism
  • M. Sakaguchi
  • Medicine, Chemistry
  • Applied Microbiology and Biotechnology
  • 2020
Diverse and common features of trehalases within different GH families and their contributions to microbial trehalose metabolism are focused on. Expand