Metabolism of Propionic Acid in Animal Tissues

Cannata, Joaquı́n J.B.; Focesi, Aldo; Mazumder, Rajarshi; Warner, Robert C.; Ochoa, Severo

doi:10.1016/s0021-9258(18)97211-x

Cited by 109 publications

(10 citation statements)

References 22 publications

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“…From these results, it is concluded that coenzyme analogs such as cyanocobalamin bind to the apoenzyme at the active site in a manner similar to that of the binding of coenzyme Bl2, and that the mercurial-sensitive sulfhydryl group(s) of the enzyme are required for the binding. It has been observed that the inhibition of Lactobacillus 208-A glycerol dehydratase as well as of a mammalian methylmalonyl-CoA mutase by mercurial compounds can be relieved by coenzyme Bi2 (Smiley and Sobolov, 1962;Cannata et al, 1965). In contrast to our observation, coenzyme B[2 can be bound by the pHMB-blocked apoenzyme of the latter in a manner that protects the cofactor from photoinactivation (Cannata et al, 1965).…”

Section: Discussioncontrasting

confidence: 75%

“…It has been observed that the inhibition of Lactobacillus 208-A glycerol dehydratase as well as of a mammalian methylmalonyl-CoA mutase by mercurial compounds can be relieved by coenzyme Bi2 (Smiley and Sobolov, 1962;Cannata et al, 1965). In contrast to our observation, coenzyme B[2 can be bound by the pHMB-blocked apoenzyme of the latter in a manner that protects the cofactor from photoinactivation (Cannata et al, 1965). Switzer and Barker (1967) have reported that the sulfhydryl protein component of the glutamate mutase system increases the affinity of the cobamide binding protein moiety for coenzyme Bi2.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Coenzyme B12 dependent propanediol dehydratase system. Nature of cobalamin binding and some properties of apoenzyme-coenzyme B12 analog complexes

Toraya¹,

Kondo²,

Isemura³

et al. 1972

Biochemistry

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New information regarding the binding of coenzyme B12 analogs to propanediol dehydratase was obtained from a study of apoenzyme-coenzyme Bi2 analog complexes which may be used as a model for the holoenzyme. Requirements for the binding of some coenzyme analogs, such as cyano-and methylcobalamin, to the apoenzyme were the same as those for coenzyme B22 binding. A monovalent cation such as potassium ion was absolutely required; the substrate also facilitated the binding, but to a lesser degree. Cyanocobalamin was bound to the apoenzyme to approximately the same extent as coenzyme B12. Treatment of the apoenzyme with a sulfhydryl inhibitor, p-chloromercuribenzoate, caused a remarkable inhibition of the binding of these cobalamins. The apoenzyme-cyanocobalamin and apoenzymemethylcobalamin complexes, like the holoenzyme, resisted inactivation by p-chloromercuribenzoate. These results suggest that the binding of coenzyme B22 to the apoenzyme is similar to the binding of these coenzyme analogs, and that c X^Voenzyme B,»* 1 dependent propanediol dehydratase (dl-1,2-propanediol hydro-lyase, EC 4.2.1.28) from Aerobacter aerogenes catalyzes the conversion of l-or d-1,2-propanediol to propionaldehyde and of 1,2-ethanediol to acetaldehyde (Lee and Abeles, 1963). Some analogs of coenzyme Bí2, such as cyano-, hydroxo-, and methylcobalamin, inhibit coenzyme B12 requiring enzymes, such as propanediol dehydratase (Lee and Abeles, 1963), glycerol dehydratase (Pawelkiewicz and Schneider, 1967), and ethanolamine deaminase (Kaplan and Stadtman, 1968b;Babior, 1969), very strongly and almost irreversibly. It has been generally accepted that the powerful inhibition by these cobalamins is due to their tight binding to an apoenzyme, forming inactive, undissociable apoenzymecoenzyme analog complexes. These complexes themselves are catalytically inactive, and no method for resolving the complexes into the native apoenzyme and cobalamin under mild conditions has hitherto been found. Therefore, the properties of apoenzyme-coenzyme Bi2 analog complexes remain almost unknown in any coenzyme Bi2 dependent enzymes, except for some properties of the glycerol dehydratase apoenzyme-hydroxocobalamin complex (Schneider et al., 1970).

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Section: Discussioncontrasting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

Coenzyme B12 dependent propanediol dehydratase system. Nature of cobalamin binding and some properties of apoenzyme-coenzyme B12 analog complexes

Toraya¹,

Kondo²,

Isemura³

et al. 1972

Biochemistry

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“…The enzyme methylmalonyl-CoA mutase is noteworthy as an AdoCblm-dependent enzyme that is found in mammals. 114 Methionine synthase is a MetCblm-dependent methyl transferase that is found in bacteria and mammals. 115 It is important in the conversion of homocysteine to methionine in the cycling of the potent methylating agent, S-adenosylmethionine (SAM).…”

Section: Continuous-wave Photolysismentioning

confidence: 99%

Magnetic Field Effects in Biology: A Survey of Possible Mechanisms with Emphasis on Radical-Pair Recombination

Grissom¹

1995

Chem. Rev.

378

272

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“…Studies from several laboratories have suggested that enzyme sulfhydryl groups may be important functional entities in corrinoid-dependent catalysis. Thus, the apoenzyme forms of diol dehydrase (Lee & Abeles, 1963) and methylmalonyl-CoA mutase (Cannata et al, 1965) are sensitive to p-(hydroxymercuri) benzoate and other sulfhydryl group reagents whereas the holoenzymes that contain Ado-Cbl are protected from inactivation by these compounds. Moreover, several corrinoid-dependent enzyme systems contain subunits that have been characterized as "thiol proteins" and that are essential for activity.…”

mentioning

confidence: 99%

Catalysis of thiol oxidation by cobalamins and cobinamides: reaction products and kinetics

Jacobsen¹,

Troxell²,

Brown³

1984

Biochemistry

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Metabolism of Propionic Acid in Animal Tissues

Cited by 109 publications

References 22 publications

Coenzyme B12 dependent propanediol dehydratase system. Nature of cobalamin binding and some properties of apoenzyme-coenzyme B12 analog complexes

Coenzyme B12 dependent propanediol dehydratase system. Nature of cobalamin binding and some properties of apoenzyme-coenzyme B12 analog complexes

Magnetic Field Effects in Biology: A Survey of Possible Mechanisms with Emphasis on Radical-Pair Recombination

Catalysis of thiol oxidation by cobalamins and cobinamides: reaction products and kinetics

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