D-3-phosphoglycerate:NAD+ oxidoreductase
3-phosphoglycerate:NAD+ 2-oxidoreductase
Glycine, serine and threonine metabolism
D-3-phosphoglycerate dehydrogenase from Escherichia coli: isolation by affinity chromatography and sequence comparison to other dehydrogenases.
Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.
The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase.
A new family of 2-hydroxyacid dehydrogenases.
Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12.
Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding.
The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues.
A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme.
Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase.
Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues.
Phosphate ion partially relieves the cooperativity of effector binding in D-3-phosphoglycerate dehydrogenase without altering the cooperativity of inhibition.
The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase.
The relationship between effector binding and inhibition of activity in D-3-phosphoglycerate dehydrogenase.
Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects.
Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase.
Molecular cloning, sequence and characterization of a novel streptococcal phosphoglycerate dehydrogenase gene.
Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.
Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.
3-Phosphoglycerate dehydrogenase from Corynebacterium glutamicum: the C-terminal domain is not essential for activity but is required for inhibition by L-serine.
De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal. Eur J Biochem. 2002 Sep;269(17):4176-84.
Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.
Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
Multiconformational states in phosphoglycerate dehydrogenase.
Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.