triose phosphate isomerase/dental caries

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Identification of the target amino acids in the site-specific inactivation of triose phosphate isomerase by ferrate anion.

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Ferrate anion, an analog of orthophosphate anion, very rapidly inactivates triose phosphate isomerase from chicken muscle. The inactivation can be prevented by the presence of competitive inhibitors. Of the 247 amino acids known to be present in each of the identical monomers of this dimeric enzyme,

A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis.

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Imidazolonepropionase (EC 3.5.2.7) catalyzes the third step in the universal histidine degradation pathway, hydrolyzing the carbon-nitrogen bonds in 4-imidazolone-5-propionic acid to yield N-formimino-l-glutamic acid. Here we report the crystal structures of the Bacillus subtilis

Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily.

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The 3.0-A-resolution x-ray structure of rat liver 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3 alpha-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an alpha/beta or triose-phosphate

Immunoproteomics reveals that cancer of the tongue and the gingivobuccal complex exhibit differential autoantibody response.

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Autoantibody response to tumor antigens has been widely used to identify novel tumor markers for different cancers, including that of the head and neck. The oral cavity, which is in the head and neck region, comprises of many sub sites with distinct biologies and incidence of cancer of each sub site

Transient expression of Ym1, a heparin-binding lectin, during developmental hematopoiesis and inflammation.

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Ym1, a secretory protein transiently produced by activated peritoneal macrophages elicited by parasitic infections, has been identified as a novel heparin-binding lectin. X-ray crystallography study revealed that Ym1 has a beta/alpha barrel structure with a carbohydrate-binding cleft similar to that

Functional analysis of Glu380 and Leu383 of soybean beta-amylase. A proposed action mechanism.

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Soybean beta-amylase, comprising a (beta/alpha)8-barrel core with a mobile loop, similar to that of triose phosphate isomerase, was mutated by site-directed mutagenesis at residues Glu380 and Leu383. X-ray crystallographic findings suggest that Glu380 is the counterpart of the catalytic site

X-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritima.

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Maturation of the [FeFe]-hydrogenase active site depends on at least the expression of three gene products called HydE, HydF, and HydG. We have solved the high resolution structure of recombinant, reconstituted S-adenosine-L-methionine-dependent HydE from Thermotoga maritima. Besides the conserved

Water-soluble vitamins for controlling starch digestion: Conformational scrambling and inhibition mechanism of human pancreatic α-amylase by ascorbic acid and folic acid.

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The inhibition of human pancreatic α-amylase (HPA) enzyme activity can offer facile routes to ameliorate postprandial hyperglycemia in diabetes via control of starch digestion. The present study utilizes complementary experimental (starch digestion kinetics, fluorescence quenching, Förster resonance

Crystal structure of D-Hydantoinase from Burkholderia pickettii at a resolution of 2.7 Angstroms: insights into the molecular basis of enzyme thermostability.

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D-Hydantoinase (D-HYD) is an industrial enzyme that is widely used in the production of D-amino acids which are precursors for semisynthesis of antibiotics, peptides, and pesticides. This report describes the crystal structure of D-hydantoinase from Burkholderia pickettii (HYD(Bp)) at a 2.7-A

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