Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2.
The glycerate kinase of a serine-producing methylotroph, Hyphomicrobium methylovorum GM2, was purified to complete homogeneity and characterized, the first time for an enzyme from a methylotroph. The enzyme was a monomer with a molecular mass about 41-52 kDa. The enzyme was stable against heating at 35 degrees C for 30 min at pH values over 6-10. Maximum activity was observed at pH 8.0 and around 50 degrees C. The Km values for D-glycerate and ATP were 0.13 mM and 0.13 mM, respectively. The enzyme showed high specificity for D-glycerate, and was activated by potassium and ammonium ions. The reaction product of the enzyme was identified as 2-phosphoglycerate.
Yoshida
T
T
Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nara, Japan.
Fukuta
K
K
Mitsunaga
T
T
Yamada
H
H
Izumi
Y
Y
D001419:Bacteria / Q000201:enzymology*; D002413:Cations, Divalent; D002414:Cations, Monovalent; D002845:Chromatography; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D017886:Durapatite; D006882:Hydroxyapatites; D007700:Kinetics; D008970:Molecular Weight; D010770:Phosphotransferases / Q000302:isolation & purification* / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor); D012694:Serine / Q000096:biosynthesis*; D013379:Substrate Specificity
D002413:Cations, Divalent; D002414:Cations, Monovalent; D006882:Hydroxyapatites; D012694:Serine; D017886:Durapatite; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C020670:glycerate kinase