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The FASEB Journal, Vol 7, 1344-1353, Copyright © 1993 by The Federation of American Societies for Experimental Biology
REVIEWS |
RH Allen, SP Stabler, DG Savage and J Lindenbaum
Department of Medicine, University of Colorado Health Sciences Center, Denver 80262.
Mammalian cells contain two Cbl-dependent enzymes, L-methylmalonyl-CoA mutase and methionine synthase. The former requires adenosyl-Cbl and catalyzes the conversion of L-methylmalonyl-CoA to succinyl-CoA. The latter requires CH3-Cbl and catalyzes the conversion of 5-CH3- tetrahydrofolate and homocysteine to tetrahydrofolate and methionine, respectively. Biochemical abnormalities related to a decrease in the activity of methionine synthase are thought to be responsible for the indistinguishable hematologic abnormalities seen in both Cbl and folate deficiency. The biochemical basis for the neuropsychiatric abnormalities seen in Cbl deficiency, but not in folate deficiency, is not known although hypotheses have been proposed that implicate one or the other of the two Cbl-dependent enzymes. Recent studies have shown that levels of serum methylmalonic acid, 2-methylcitric acids I and II, total homocysteine, and cystathionine are elevated in most patients with Cbl deficiency and that total homocysteine, cystathionine, N,N- dimethylglycine, and N-methylglycine are elevated in most patients with folate deficiency. Analysis of these metabolic abnormalities in various patient groups fails to support hypotheses that either L-methylmalonyl- CoA mutase or methionine synthase alone are responsible for the neuropsychiatric abnormalities. We suggest that they may result from a third, unknown mammalian Cbl-dependent enzyme or from a combined deficiency of both Cbl-dependent enzymes together with an unknown genetic or environmental factor.
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