Disulfide reduction and sulfhydryl oxidation by microbial enzyme. III. Purification of thiol-disulfide interchange enzyme from Candida claussenii.
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Purification and properties of an enzyme from beef liver which catalyzes sulfhydryl-disulfide interchange in proteins.
An enzyme which catalyzes sulfhydryl-disulfide interchange in proteins containing “incorrect” disulfide bonds has been isolated from beef liver microsomes. The purified form of this enzyme shows two bands upon electrophoresis in starch gels and polyacrylamide gels. The proteins represented by these bands are considered to be variants of the same protein because both are enzymically active after...
متن کاملParticipation of the unsymmetrical disulfide of coenzyme A and glutathione in an enzymatic sulfhydryl-disulfide interchange. I. Partial purification and properties of the bovine kidney enzyme.
In addition, it has been detected in most rat tissues studied. Its pH optimum is 8.2 and the equilibrium constant for the reaction is near unity at pH 6.9 and 25’. Michaelis constants for reduced glutathione and CoASSG are 3.3 x 10-4?d and 4.5 x 10-5b& respectively. The molecular weight of the enzyme, determined by gel filtration, is approximately 12,000. Several unsymmetrical disulfides contai...
متن کاملThiol/disulfide exchange between rabbit muscle phosphofructokinase and glutathione. Kinetics and thermodynamics of enzyme oxidation.
Reversible thiol/disulfide exchange equilibria between rabbit muscle phosphofructokinase and glutathione redox buffers results in a dependence of the activity of the enzyme on the thiol to disulfide ratio of the redox buffer (Gilbert, H. F. (1982) J. Biol. Chem. 257, 12086-12091). The transition between fully reduced (active) and fully oxidized (inactive) enzyme is half complete at a [GSH]/[GSS...
متن کاملSulfur shuffle: modulating enzymatic activity by thiol-disulfide interchange.
The facile modulation of biological processes is an important goal of biological chemists. Here, a general strategy is presented for controlling the catalytic activity of an enzyme. This strategy is demonstrated with ribonuclease A (RNase A), which catalyzes the cleavage of RNA. The side-chain amino group of Lys41 donates a hydrogen bond to a nonbridging oxygen in the transition state for RNA c...
متن کاملProtection of the Queuosine Biosynthesis Enzyme QueF from Irreversible Oxidation by a Conserved Intramolecular Disulfide
QueF enzymes catalyze the nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of the nitrile group of 7-cyano-7-deazaguanine (preQ₀) to 7-aminomethyl-7-deazaguanine (preQ₁) in the biosynthetic pathway to the tRNA modified nucleoside queuosine. The QueF-catalyzed reaction includes formation of a covalent thioimide intermediate with a conserved active site cysteine that is pro...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1975
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.39.1417