Some properties of D-mannose isomerase from Escherichia coli K12. 1981

F J Stevens, and P W Stevens, and J G Hovis, and T T Wu

A second-stage mutant of Escherichia coli K12 designated as strain 806 grew faster on D-lyxose than the mutant strain 805 previously described. Both mutants produced constitutively a novel enzyme, D-mannose isomerase, but strain 806 produced twice as much as strain 805. The enzyme could fortuitously convert D-lyxose to D-xylulose, which is a normal intermediate in the D-xylose catabolic pathway. The purified enzyme consisted of four subunits each with a molecular weight of about 40 000. In 0.14 M-Na2SO4, the tetramer dissociated completely into dimers. While the tetramer Km values for D-mannose and D-lyxose were 80 mM and 300 mM, respectively, the dimer Km values for these two sugars were both 300 mM. The amino acid composition of the enzyme was also determined.

UI MeSH Term Description Entries
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D002238 Carbohydrate Epimerases Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3. Carbohydrate Isomerases,Epimerases, Carbohydrate,Isomerases, Carbohydrate
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D012964 Sodium A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23. Sodium Ion Level,Sodium-23,Ion Level, Sodium,Level, Sodium Ion,Sodium 23
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D013431 Sulfates Inorganic salts of sulfuric acid. Sulfate,Sulfates, Inorganic,Inorganic Sulfates
D019747 Aldose-Ketose Isomerases Enzymes that catalyze the interconversion of aldose and ketose compounds. Ketose-Aldose Isomerases,Aldose Ketose Isomerases,Isomerases, Aldose-Ketose,Isomerases, Ketose-Aldose,Ketose Aldose Isomerases

Related Publications

F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
October 2018, Journal of the science of food and agriculture,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
April 1986, Biochimica et biophysica acta,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
June 1973, Biochimica et biophysica acta,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
March 1972, European journal of biochemistry,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
February 1973, Journal of bacteriology,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
March 1976, The Biochemical journal,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
May 2021, Applied biochemistry and biotechnology,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
January 2009, Prikladnaia biokhimiia i mikrobiologiia,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
August 1996, European journal of biochemistry,
F J Stevens, and P W Stevens, and J G Hovis, and T T Wu
April 1992, Protein engineering,
Copied contents to your clipboard!