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The Structure of Pea Alcohol Dehydrogenase Using Inactivation by Iodoacetate
Author(s) -
LAPKA ROMAN,
LEBLOVÁ SYLVA
Publication year - 1977
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.1399-3054.1977.tb09289.x
Subject(s) - nad+ kinase , cofactor , alcohol dehydrogenase , biochemistry , nucleotide , binding site , chemistry , pisum , chelation , dehydrogenase , enzyme , stereochemistry , inorganic chemistry , gene
Abstract Alcohol dehydrogenase (E.C. 1.1.1.1, abbreviated ADH) isolated from germinating pea seeds ( Pisum arvense L.) is inactivated by iodoacetate. The inactivation rate is decreased by ATP, ADP, AMP, NAD, chloride ions and o ‐phenanthroline. The nucleotides studied are bound in the area of the coenzyme binding site, similar to iodoacetate. On the other hand, o ‐phenanthroline binds zinc ions in a chelate which is apparently bound in the close vicinity of the coenzyme binding site.