Ethanolamine ammonia-lyase: inactivation of the holoenzyme by N2O and the mechanism of action of Coenzyme B12

Bioinorganic Chemistry
G N Schrauzer, E A Stadlbauer

Abstract

Functional ethanolamine ammonia-lyase is inactivated by N2O as well as by O2, indicating that the active form of coenzyme B12 is an enzyme-bound corrin derivative in which the Co-C bond of the coenzyme is broken and the cobalt ion is in the +1 state of oxidation. The nucleoside fragment formed in the process of coenzyme activation is tentatively identified as 4',5'-didehydro-5'-deoxyadenosine. A mechanism of action of ethanolamine ammonia-lyase is formulated in analogy to that of DL-1,2-Propanediol dehydrase and compared to proposed alternative reaction schemes.

References

Aug 1, 1979·British Journal of Haematology·M H CullenJ A Amess
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Jan 1, 1979·CRC Critical Reviews in Biochemistry·B M Babior, J S Krouwer
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Citations

Dec 1, 1987·Blood Reviews·B M Babior, J T Curnutte
Aug 11, 1971·Journal of the American Chemical Society·G N Schrauzer, R J Holland
Feb 25, 1970·Journal of the American Chemical Society·G N Schrauzer, J W Sibert
Mar 10, 1971·Journal of the American Chemical Society·M K EssenbergR H Abeles
May 7, 1969·Journal of the American Chemical Society·J H BaystonM E Winfield
Nov 5, 1965·Journal of the American Chemical Society·T C French, G G Hammes

Related Concepts

Propylene Glycol
Ethanolamine Ammonia-Lyase
Plasma Protein Binding Capacity
Oxidation
Ammonia-Lyases
Clostridium
Cobamamide
Ethanolamines
Nucleosides
Eritron

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