Results 111 to 120 of about 636 (121)
Involvement of Glucosamine 6 Phosphate Isomerase 2 (GNPDA2) Overproduction in β-Amyloid- and Tau P301L-Driven Pathomechanisms. [PDF]
BiomoleculesLachén-Montes M +8 more
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Efficient enzymatic synthesis of L-rhamnulose and L-fuculose. [PDF]
Bioorg Med Chem Lett, 2016 Wen L +5 more
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Benchmarking predictive methods for small-angle X-ray scattering from atomic coordinates of proteins using maximum likelihood consensus data. [PDF]
IUCrJTrewhella J, Vachette P, Larsen AH.
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International Journal of Mass Spectrometry, 2005
Abstract A mass spectrometry based method for the direct determination of kinetic constants for phosphoglucose isomerase (PGI) and phosphomannose isomerase (PMI) is described. PGI catalyzes the interconversion between glucose-6-phosphate (Glc6P) and fructose-6-phosphate (Fru6P) and PMI performs the same function between mannose-6-phosphate (Man6P ...
Hong Gao, Ye Chen, Julie A. Leary
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Abstract A mass spectrometry based method for the direct determination of kinetic constants for phosphoglucose isomerase (PGI) and phosphomannose isomerase (PMI) is described. PGI catalyzes the interconversion between glucose-6-phosphate (Glc6P) and fructose-6-phosphate (Fru6P) and PMI performs the same function between mannose-6-phosphate (Man6P ...
Hong Gao, Ye Chen, Julie A. Leary
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Journal of Molecular Biology, 1990
The active site and mechanism of D-xylose isomerase have been probed by determination of the crystal structures of the enzyme bound to various substrates, inhibitors and cations. Ring-opening is an obligatory first step of the reaction and is believed to be the rate-determining step for the aldose to ketose conversion. The structure of a complex with a
C A, Collyer, K, Henrick, D M, Blow
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The active site and mechanism of D-xylose isomerase have been probed by determination of the crystal structures of the enzyme bound to various substrates, inhibitors and cations. Ring-opening is an obligatory first step of the reaction and is believed to be the rate-determining step for the aldose to ketose conversion. The structure of a complex with a
C A, Collyer, K, Henrick, D M, Blow
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Journal of Molecular Biology, 2008
The three-dimensional structure of a Salmonella enterica hypothetical protein YihS is significantly similar to that of N-acyl-D-glucosamine 2-epimerase (AGE) with respect to a common scaffold, an alpha6/alpha6-barrel, although the function of YihS remains to be clarified. To identify the function of YihS, Escherichia coli and S.
Takafumi, Itoh +3 more
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The three-dimensional structure of a Salmonella enterica hypothetical protein YihS is significantly similar to that of N-acyl-D-glucosamine 2-epimerase (AGE) with respect to a common scaffold, an alpha6/alpha6-barrel, although the function of YihS remains to be clarified. To identify the function of YihS, Escherichia coli and S.
Takafumi, Itoh +3 more
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1972
Publisher Summary This chapter describes the molecular and catalytic properties of aldose–ketose isomerases. Aldose–ketose isomerases catalyze the interconversion of isomeric aldo- and keto sugars by causing the migration of carbon-bound hydrogen between carbons 1 and 2.
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Publisher Summary This chapter describes the molecular and catalytic properties of aldose–ketose isomerases. Aldose–ketose isomerases catalyze the interconversion of isomeric aldo- and keto sugars by causing the migration of carbon-bound hydrogen between carbons 1 and 2.
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Mechanism of the aldose-ketose isomerase reactions.
Advances in enzymology and related areas of molecular biology, 1976openaire +1 more source