Substrate Inhibition ofd-Amino Acid Transaminase and Protection by Salts and by Reduced Nicotinamide Adenine Dinucleotide:  Isolation and Initial Characterization of a Pyridoxo Intermediate Related to Inactivation†

Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 2879-2888 ◽  
Author(s):  
Peter W. van Ophem ◽  
Shawn D. Erickson ◽  
Alvaro Martinez del Pozo ◽  
Ivan Haller ◽  
Brian T. Chait ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Substrate Inhibition ◽  
Nicotinamide Adenine ◽  
Initial Characterization ◽  
Reduced Nicotinamide Adenine Dinucleotide

CHARACTERIZATION OF A NICOTINAMIDE ADENINE DINUCLEOTIDE SPECIFIC NITRITE REDUCTASE FROM ESCHERICHIA COLI, STRAIN K12

1963 ◽  
Vol 9 (4) ◽  
pp. 531-539 ◽  
Author(s):  
Donald P. Zarowny ◽  
B. D. Sanwal
Keyword(s):  
Escherichia Coli ◽  
Nitrite Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Enzymic Activity ◽  
Coli Strain ◽  
Nicotinamide Adenine ◽  
Optimum Ph ◽  
Michaelis Constants ◽  
Reduced Nicotinamide Adenine Dinucleotide

A nitrite reductase specific for reduced nicotinamide adenine dinucleotide (NADH) was purified approximately 30-fold from Escherichia coli, strain K12. The enzyme was metal sensitive, being inhibited by certain chelating agents and stimulated by others. The optimum pH for enzymic activity was 7.8–8.0 and the Michaelis constants for nitrite and NADH were 4.0 × 10−5 moles/l, and 3.3 × 10−4 moles/l., respectively. The partially purified enzyme did not show a flavin requirement and ammonia was not the product of the enzymic reaction.

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