The mechanism of adduct formation between NAD+ and pyruvate bound to pig heart lactate dehydrogenase
Keyword(s):
1. The rate of adduct formation between NAD+ and enol-pyruvate at the active site of lactate dehydrogenase is determined by the rate of enolization of pyruvate in solution. 2. The proportion of enol-pyruvate solutions is less than 0.01%. 3. The overall dissociation constant of adduct formation is less than 5 × 10(-8) M for pig heart lactate dehydrogenase at pH 7.0. 4. The unusual kinetics for adduct formation previously observed in the case of rabbit muscle lactate dehydrogenase [Griffin & Criddle (1970) Biochemistry 9, 1195–1205] may be attributed to the concentration of enol-pyruvate in solution being considerably less than the concentration of enzyme.
1962 ◽
Vol 237
(5)
◽
pp. 1668-1675
1978 ◽
Vol 26
(1)
◽
pp. 130-133
◽
1977 ◽
Vol 14
(1-6)
◽
pp. 48-52
◽
Keyword(s):
1978 ◽
Vol 56
(8)
◽
pp. 774-779
◽
1982 ◽
Vol 216
(1)
◽
pp. 329-336
◽
Keyword(s):
1964 ◽
Vol 85
(2)
◽
pp. 177-185
1998 ◽
Vol 74
(5)
◽
pp. 2666-2673
◽
1974 ◽
Vol 359
(2)
◽
pp. 288-297
◽