Diacetyl (Acetoin) Reductase from Aerobacter aerogenes. Structural Properties
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چکیده
منابع مشابه
D-apiose reductase from Aerobacter aerogenes.
A strain of Aerobacter aerogenes PRL-R3 has been isolated which utilizes d-apiose as its sole source of carbon. A new enzyme, d-apiose reductase, was discovered in this strain. The enzyme was not present when the strain was grown on d-glucose. d-Apiose reductase catalyzes the nicotinamide adenine dinucleotide-dependent interconversion of d-apiose and d-apiitol. The enzyme is specific for d-apio...
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The enzyme D-ribulokinase from Aerobacter aerogenes was purified to near homogeneity. The molecular weight, as determined by Sephacryl gel chromatography, is 116,000. The subunit molecular weight, determined by sodium dodecyl sulfate-gel electrophoresis, is 59,000, suggesting that D-ribulokinase is a dimer of identical subunits. Initial rate kinetic studies, involving substrate analogs and prod...
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A plasmid-borne diacetyl (acetoin) reductase (butA) from Leuconostoc pseudomesenteroides CHCC2114 was sequenced and cloned. Nucleotide sequence analysis revealed an open reading frame encoding a protein of 257 amino acids which had high identity at the amino acid level to diacetyl (acetoin) reductases reported previously. Downstream of the butA gene of L. pseudomesenteroides, but coding in the ...
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Two pathways for methionine methyl formation, one cobalamindependent and one cobalamin-independent, corresponding to those observed in Escherichia coli PA 15 have been found in Aerobacter aerogenes. An initial difficulty in showing the cobalamin-dependent pathway in cellfree extracts proved to be due to the presence of enzymes which caused the removal of adenosylmethionine, a cofactor required ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1971
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1971.tb01379.x