Properties of D-Xylose Isomerase from Streptomyces albus

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Published inApplied Microbiology Vol. 29; no. 6; pp. 745 - 750
Main Authors Sanchez, S, Smiley, K L
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.06.1975
Subjects
Arabinose - metabolism
Carbohydrate Epimerases - metabolism
Cell-Free System
Cobalt - pharmacology
Enzyme Activation
Glucose - metabolism
Hydrogen-Ion Concentration
Magnesium - pharmacology
Metabolism and Products
Rhamnose - metabolism
Ribose - metabolism
Soil Microbiology
Sorbitol - pharmacology
Stereoisomerism
Streptomyces - enzymology
Temperature
Xylose - metabolism
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Abstract Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue AEM About AEM Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy AEM RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0099-2240 Online ISSN: 1098-5336 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to AEM .asm.org, visit: AEM       
AbstractList A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined. D-Glucose, D-xylose, D-ribose, L-arabinose, and L-rhamnose served as substrates for the enzyme with respective K m values of 86, 93, 350, 153, and 312 mM and V max values measuring 1.23, 2.9, 2.63, 0.153, and 0.048 μmol/min per mg of protein. The hexose D-allose was also isomerized. The enzyme was strongly activated by 1.0 mM Mg 2+ but only partially activated by 1.0 mM Co 2+ . The respective K m values for Mg 2+ and Co 2+ were 0.3 and 0.003 mM. Mg 2+ and Co 2+ appear to have separate binding sites on the isomerase. These cations also protect the enzyme from thermal denaturation and from D-sorbitol inhibition. The optimum temperature for ketose formation was 70 to 80 C at pH values ranging from 7 to 9. D-Sorbitol acts as a competitive inhibitor with a K i of 5.5 mM against D-glucose, D-xylose, and D-ribose. Induction experiments, Mg 2+ activation, and D-sorbitol D-sorbitol inhibition indicated that a single enzyme (D-xylose isomerase) was responsible for the isomerization of the pentoses, methyl pentose, and glucose.
A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined. D-Glucose, D-xylose, D-ribose, L-arabinose, and L-rhamnose served as substrates for the enzyme with respective Km values of 86, 93, 350, 153, and 312 mM and Vmax values measuring 1.23, 2.9, 2.63, 0.153, and 0.048 mumol min per mg of protein. The hexose D-allose was also isomerized. The enzyme was strongly activated by 1.0 mM Mg2+ but only partially activated by 1.0 mM Co2+. The respective Km values for Mg2+ and Co2+ were 0.3 and 0.003 mM. Mg2+ and Co2+ appear to have separate binding sites on the isomerase. These cations also protect the enzyme from thermal denaturation and from D-sorbitol inhibition. The optimum temperature for ketose formation was 70 to 80 C at pH values ranging from 7 to 9. D-Sorbitol acts as a competitive inhibitor with a Ki of 5.5 mM against D-glucose, D-xylose, and D-ribose. Induction experiments, Mg2+ activation, and D-sorbitol inhibition indicated that a single enzyme (D-xylose isomerase) was responsible for the isomerization of the pentoses, methyl pentose, and glucose.
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Author Sergio Sanchez
Karl L. Smiley
AuthorAffiliation Northern Regional Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, Peoria, Illinois 61604
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Present address: Dept. of Nutrition and Food Science, M.I.T., Cambridge, Mass. 02139.
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A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined....
A partially purified D-xylose isomerase has been isolated from cells of Streptomyces albus NRRL 5778 and some of its properties have been determined....
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SubjectTerms Arabinose - metabolism
Carbohydrate Epimerases - metabolism
Cell-Free System
Cobalt - pharmacology
Enzyme Activation
Glucose - metabolism
Hydrogen-Ion Concentration
Magnesium - pharmacology
Metabolism and Products
Rhamnose - metabolism
Ribose - metabolism
Soil Microbiology
Sorbitol - pharmacology
Stereoisomerism
Streptomyces - enzymology
Temperature
Xylose - metabolism
Title Properties of D-Xylose Isomerase from Streptomyces albus
URI http://aem.asm.org/content/29/6/745.abstract
https://www.ncbi.nlm.nih.gov/pubmed/239628
https://search.proquest.com/docview/82967100
https://pubmed.ncbi.nlm.nih.gov/PMC187073
Volume 29
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