High impact information on RCJMB04_5g20

• The steady state kinetics and effects of salts on chicken breast phosphoglycerate mutase have been examined [1].
• Phosphoglycerate mutase and bisphosphoglycerate synthase (mutase) can both be phosphorylated by either glycerate-1,3-P2 or glycerate-2,3-P2 to form phosphohistidine enzymes [2].
• Rates of phosphorylation and dephosphorylation of phosphoglycerate mutase and bisphosphoglycerate synthase [2].
• The sequence of a peptide containing the active site phosphohistidine residue of phosphoglycerate mutase from chicken breast muscle [3].
• Phosphoglycerate mutase is phosphorylated on a histidine residue by the cofactor of the reaction, 2,3-bisphosphoglycerate (Rose, Z. B. (1970) Arch. Biochem. Biophys. 140, 508-513) [3].

Anatomical context of RCJMB04_5g20

• 3. Two of the fractions have glycerate-2,3-P2 synthase, glycerate-2,3-P2 phosphatase and phosphoglycerate mutase activities in a ratio similar to that of the glycerate-2,3-P2 synthase described in mammalian skeletal muscle [4].

Associations of RCJMB04_5g20 with chemical compounds

• This did not result from an increased rate of E-P breakdown, as is the case with phosphoglycerate mutase, an enzyme which shares structural and functional similarity to fructose-2,6-bisphosphate [5].
• 1. Turnover of the sarcoplasmic proteins aldolase, phosphoglycerate mutase, lactate dehydrogenase and creatine phosphokinase isolated from chicken breast muscle was investigated using a pulse labelling technique [6].
• The seven enzymes isolated were: phosphorylase, enolase, creatine-P kinase, aldolase, glyceraldehyde-3-P dehydrogenase, phosphoglycerate mutase, and triose-P isomerase [7].

References