Crystal Structure of Binary and Ternary Complexes of Serine Hydroxymethyltransferase from Bacillus stearothermophilus

Crystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate.

The crystal structure of the phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus was solved in complex with its cofactor, NAD, and its physiological substrate, D-glyceraldehyde 3-phosphate (D-G3P). To isolate a stable ternary complex, the nucleophilic residue of the active site, Cys(149), was substituted with alanine or serine. The C149A and C149S G...

Crystal structure of two ternary complexes of phosphorylating Glyceraldehyde - 3 - 1 Phosphate Dehydrogenase from Bacillus stearothermophilus with NAD and D - 2 Glyceraldehyde - 3 - Phosphate

Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding.

The crystal structure of NAD(+)-dependent alcohol dehydrogenase from Bacillus stearothermophilus strain LLD-R (htADH) was determined using X-ray diffraction data at a resolution of 2.35 A. The structure of homotetrameric htADH is highly homologous to those of bacterial and archaeal homotetrameric alcohol dehydrogenases (ADHs) and also to the mammalian dimeric ADHs. There is one catalytic zinc a...

Serine hydroxymethyltransferase from Solanum tuberosum.

SHMT, EC 2.1.2.1, catalyzes the interconversion of Ser and Gly accompanied by the production or consumption of one-carbon units. In leaves it is a component of the photorespiratory pathway (Keys et al., 1978). The main function of that pathway is the salvage of reduced carbon and nitrogen withdrawn from the Calvin cycle by the oxygenation of ribulose 1,5-bisphosphate. By the cooFeration of SHMT...

Crystal structure of binary and ternary complexes of archaeal UDP-galactose 4-epimerase-like L-threonine dehydrogenase from Thermoplasma volcanium.

A gene from the thermophilic archaeon Thermoplasma volcanium encoding an L-threonine dehydrogenase (L-ThrDH) with a predicted amino acid sequence that was remarkably similar to the sequence of UDP-galactose 4-epimerase (GalE) was overexpressed in Escherichia coli, and its product was purified and characterized. The expressed enzyme was moderately thermostable, retaining more than 90% of its act...