1. |
Niehues B,
Jossek R,
Kramer U,
Koch A,
Jarling M,
Schröder W,
Pape H,
( 2003 ) Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis. PMID : 12879214 : DOI : 10.1007/s00203-003-0575-y Abstract >>
Crude extracts of Actinoplanes missouriensis and related strains catalyze the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. The enzyme of A. missouriensis responsible for this reaction was purified and characterized. This protein has an estimated molecular mass of 57 kDa and it is most likely a monomer. The K(m) value was 2.6 mM for maltose and 0.54 mM for ATP. Only maltose acted effectively as phosphoryl-group acceptor, and ATP was not replaceable as phosphoryl-group donor. Tryptic peptides of the enzyme were sequenced, and the sequences of these peptides will allow construction of degenerate primers to identify the gene coding for this unique kinase.
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2. |
Tamura T,
Kasai H,
( 2000 ) Intrageneric relationships among Micromonospora species deduced from gyrB-based phylogeny and DNA relatedness. PMID : 10826795 : DOI : 10.1099/00207713-50-1-127 Abstract >>
The phylogenetic structure of genus Micromonospora within actinomycetes was examined by analysing the gyrB sequences of 15 validly described species and four subspecies. All but one of the Micromonospora strains formed a tight cluster, as had previously been demonstrated by a 16S rDNA-based phylogenetic analysis. However, the intrageneric relationships deduced from the gyrB-based phylogeny were different from those based on their 16S rDNA sequences. To examine which phylogeny would be more relevant for classifying genus Micromonospora, DNA-DNA hybridization experiments were performed. The gyrB-based classification agrees with the results of the DNA-DNA hybridization studies, indicating that this classification method is useful for analysing the phylogenetic relationships of high G+C Gram-positive bacteria at the level of the genomic species. Genus Micromonospora was reclassified into the following 14 species: Micromonospora echinospora, Micromonospora pallida, Micromonospora nigra, Micromonospora purpureochromogenes, Micromonospora aurantiaca, Micromonospora carbonacea, Micromonospora chalcea, Micromonospora chersina, Micromonospora coerulea, Micromonospora gallica, Micromonospora halophytica, Micromonospora inositola, Micromonospora olivasterospora and Micromonospora rosaria.
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3. |
Jarling M,
Cauvet T,
Grundmeier M,
Kuhnert K,
Pape H,
( 2004 ) Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase. PMID : 15378530 : DOI : 10.1002/jobm.200410403 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.
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4. |
Rommel TO,
Hund HK,
Speth AR,
Lingens F,
( 1989 ) Purification and N-terminal amino-acid sequences of bacterial malate dehydrogenases from six actinomycetales strains and from Phenylobacterium immobile, strain E. PMID : 2775496 : Abstract >>
Malate dehydrogenases from Streptosporangium roseum (DSM 43021), Planomonospora venezuelensis (DSM 43178), Microtetraspora glauca (ATCC 23057), Actinoplanes missouriensis (DSM 43046), Streptomyces atratus (ATCC 14046), Kibdelosporangium aridum (ATCC 39323), and from Phenylobacterium immobile, strain E (DSM 1986) were purified to homogeneity. The N-terminal amino-acid sequences were determined and compared with known prokaryotic and eukaryotic sequence data. The partial sequences from Actinomycetales enzymes include a string of amino acids which is also present in the N-terminal region of malate dehydrogenases from Thermus flavus and from mammalian cytoplasm.
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5. |
( 1996 ) Maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes sp.: demonstration of enzyme activity and characterization of the reaction product. PMID : 8690081 : DOI : 10.1016/0014-5793(96)00554-6 Abstract >>
Cell free extract of the acarbose producer Actinoplanes sp. catalyzes ATP-dependent phosphorylation of maltose. This was shown by two different assays. The product was purified and its structure determined to be alpha-maltose-1-phosphate by chemical analysis and NMR spectroscopy.
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