Purification and properties of malate synthetase from castor beans

Autor:	Yukio Yamamoto, Harry Beevers
Rok vydání:	1961
Předmět:	chemistry.chemical_classification Ricinus Malate Synthase Glyoxylate cycle General Medicine Glutathione Biology Castor Bean Malate dehydrogenase Enzymes Divalent chemistry.chemical_compound Enzyme chemistry Biochemistry Acetyl coenzyme Malate Synthetase Castor beans
Zdroj:	Biochimica et Biophysica Acta. 48:20-25
ISSN:	0006-3002
DOI:	10.1016/0006-3002(61)90510-8
Popis:	Malate synthetase has been purified some 300-fold from crude extracts of germinating castor-bean seedlings. The enzyme was completely inactive in the absence of divalent cations and was maximally activated by Mg++. The Km for acetyl coenzyme A was 6.7 · 10−5M and that for glyoxylate was 8.5 · 10−5M. None of a variety of aldehydes substituted for glyoxylate. No evidence was obtained that the enzyme could catalyze the breakdown of malate.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9960e02e3cace4f7244160aa4759732 https://doi.org/10.1016/0006-3002(61)90510-8 Zobrazit plný text záznamu