Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme

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Manganese transport in Brevibacterium ammoniagenes ATCC 6872.

Uptake of manganese by Brevibacterium ammoniagenes ATCC 6872 was energy dependent and obeyed saturation kinetics (Km = 0.65 microM; Vmax = 0.12 mumol/min per g [dry weight]). Uptake showed optima at 27 degrees C and pH 9.5. 54Mn2+ accumulated by the cells was released by treatment with toluene or by exchange for unlabeled manganese ions, via an energy-dependent process. Co2+, Fe2+, Cd2+, and Zn...

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The active form of the R2F protein of class Ib ribonucleotide reductase from Corynebacterium ammoniagenes is a diferric protein.

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NrdH-Redoxin Protein Mediates High Enzyme Activity in Manganese-reconstituted Ribonucleotide Reductase from Bacillus anthracis*

Bacillus anthracis is a severe mammalian pathogen encoding a class Ib ribonucleotide reductase (RNR). RNR is a universal enzyme that provides the four essential deoxyribonucleotides needed for DNA replication and repair. Almost all Bacillus spp. encode both class Ib and class III RNR operons, but the B. anthracis class III operon was reported to encode a pseudogene, and conceivably class Ib RNR...

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Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.

Bacillus subtilis class Ib ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, providing the building blocks for DNA replication and repair. It is composed of two proteins: α (NrdE) and β (NrdF). β contains the metallo-cofactor, essential for the initiation of the reduction process. The RNR genes are organized within the nrdI-nrdE-nrdF-ymaB operon. Each p...

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Production of Coenzyme A by a Mutant of Brevibacterium ammoniagenes Resistant to Oxypantetheine.

For improved production of coenzyme A (CoA), a mutant of Brevibacterium ammoniagenes IFO127071 resistant to oxypantetheine, the corresponding oxygen analog of pantetheine, was obtained. In the mutant, activity of pantothenate kinase (EC 2.7.1.33), the first-step enzyme for the biosynthesis of CoA from pantothenic acid, l-cysteine, and ATP, was about threefold higher than that in the parent stra...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1988

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1988.tb13740.x