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Glycerate kinase from spinach leaves: Partial purification, characterization and subcellular localization
Author(s) -
Chaguturu Rathnam
Publication year - 1985
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1985.tb02812.x
Subject(s) - spinacia , spinach , stereospecificity , enzyme , divalent , biochemistry , chloroplast , enantiomer , biology , cytosol , chemistry , stereochemistry , catalysis , organic chemistry , gene
Spinach ( Spinacia oleracea L. cv. Melody hybrid) leaf glycerate kinase (EC 2.7.1.31) was partially purified and characterized. The enzyme did not exhibit any absolute stereospecificity towards the two enantiomers of glycerate, but the affinity for the D‐isomer was 15‐fold greater. The enzyme exhibited a broad pH optimum of 7.5–9.0 and a requirement for divalent cation, satisfied by Mg 2+ . The reaction product was identified as 3‐phosphoglyceric acid. The observed high glycerate kinase activity together with its strategic localization exclusively in the chloroplast stroma are considered adequate for an efficient coupling of photosynthetic and photorespiratory carbon pathways.