Complex formation of apoenzyme, coenzyme and substrate of d-amino acid oxidase V. Change in conformation of the protein by forming a model of enzyme-substrate complex

1963 ◽  
Vol 77 ◽  
pp. 20-26 ◽  
Author(s):  
Kunio Yagi ◽  
Takayuki Ozawa ◽  
Tatsuo Ooi
Keyword(s):  
Amino Acid ◽  
Complex Formation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Substrate Complex ◽  
Enzyme Substrate

Complex Formation between Reduced D-Amino Acid Oxidase and Pyridine Carboxylates1

1986 ◽  
Vol 99 (3) ◽  
pp. 673-680 ◽  
Author(s):  
Yasuzo NISHINA ◽  
Hiromasa TOJO ◽  
Kiyoshi SHIGA
Keyword(s):  
Amino Acid ◽  
Complex Formation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals OPHIDIAN l-AMINO ACID OXIDASE. THE NATURE OF THE ENZYME-SUBSTRATE COMPLEXES

1965 ◽  
Vol 95 (1) ◽  
pp. 262-269 ◽  
Author(s):  
EA ZELLER ◽  
G RAMACHANDER ◽  
GA FLEISHER ◽  
T ISHIMARU ◽  
V ZELLER
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Enzyme Substrate

scholarly journals The carbanion of nitroethane is an inhibitor of, and not a substrate for, flavocytochrome b2 [l-(+)-lactate dehydrogenase]

1990 ◽  
Vol 266 (1) ◽  
pp. 301-304 ◽  
Author(s):  
R Genet ◽  
F Lederer
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Active Site ◽  
Competitive Inhibitor ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Flavocytochrome B2 ◽  
Enzyme Substrate

Although nitroethane does not bind to the active site of flavocytochrome b2, its anion, ethane nitronate, behaves as a competitive inhibitor, with a Ki of 2.2 mM. No electron transfer can be detected between the nitronate and the enzyme, in contrast with the observations of other workers on D-amino acid oxidase. Propionate is a competitive inhibitor, with a Ki of 28 mM. The significance of these results with respect to the proposed carbanion mechanism and the putative existence of a covalent enzyme-substrate intermediate is discussed.

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