Nicotinic Acid Metabolism, V. A Cobamide Coenzyme-Dependent Conversion of α-Methyleneglutaric Acid to Dimethylmaleic Acid | Zendy

HsiangFu Kung | Zendy; Stephen Cederbaum | Zendy; LiKai Tsai | Zendy; Thressa C. Stadtman | Zendy

Open Access

Nicotinic Acid Metabolism, V. A Cobamide Coenzyme-Dependent Conversion of α-Methyleneglutaric Acid to Dimethylmaleic Acid

Author(s) -

HsiangFu Kung,

Stephen Cederbaum,

LiKai Tsai,

Thressa C. Stadtman

Publication year - 1970

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.65.4.978

Subject(s) - chemistry , propionate , ammonia , organic chemistry , cofactor , isomerization , metabolism , catalysis , biochemistry , enzyme

A new B12 -coenzyme-dependent isomerization, catalyzed by extracts of a nicotinate-fermenting clostridium, results in the conversion of α-methyleneglutaric acid to dimethylmaleic acid. These two acids are intermediates in the multistep anaerobic process wherein nicotinate is converted, ultimately, to one mole each of propionate, acetate, carbon dioxide, and ammonia.Dimethylmaleic acid reacts in its anhydride form with 2,4-dinitrophenylhydrazine to formN -2′,4′-dinitrophenyl-anilino-3,4-dimethylmaleimide. The characteristic reddish color exhibited by the latter derivative in alkaline solution serves as a convenient quantitative assay for dimethylmaleic acid. Comparison of the 2,4-dinitrophenylhydrazine derivatives of the product of the enzymic reaction and of synthetic dimethylmaleic anhydride showed them to be identical in every respect.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research