Literature DB >> 5874535

Glucosamine-6-phosphate degradation by Proteus vulgaris and isolation of phosphoglucosaminisomerase.

H Aron, H H Yonenaka, H I Nakada.   

Abstract

Aron, H. (University of California, Santa Barbara), H. H. Yonenaka, and H. I. Nakada. Glucosamine-6-phosphate degradation by Proteus vulgaris and isolation of phosphoglucosaminisomerase. J. Bacteriol. 87:1123-1128. 1964.-The presence of the enzyme, phosphoglucosaminisomerase, was demonstrated in a strain of Proteus vulgaris. Fructose-6-phosphate and ammonia were shown to be the primary reaction products. The optimal pH was 7.2 with a broad peak. This differs from previously reported bacterial phosphoglucosaminisomerases which had a pH optimum of about 5.8. Other properties of the enzyme are presented.

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Year:  1964        PMID: 5874535      PMCID: PMC277156          DOI: 10.1128/jb.87.5.1123-1128.1964

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  14 in total

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8.  The chromatographic determination of glucosamine with ninhydrin.

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9.  The phosphorylation of D (+) glucosamine by crystalline yeast hexokinase.

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10.  Glucosamine degradation by Escherichia coli. II. The isomeric conversion of glucosamine 6-PO4 to fructose 6-PO4 and ammonia.

Authors:  H I NAKADA; J B WOLFE
Journal:  Arch Biochem Biophys       Date:  1956-10       Impact factor: 4.013

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