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ACADM wt Allele

Known as: FLJ99884, FLJ18227, FLJ93013 
Human ACADM wild-type allele is located in the vicinity of 1p31 and is approximately 39 kb in length. This allele, which encodes medium-chain… Expand
National Institutes of Health

Related topics

Related topics

6 relations

Broader (1)

ACADM gene
CDH15 geneMedium-Chain Specific Acyl-CoA Dehydrogenase, MitochondrialMedium-chain acyl-coenzyme A dehydrogenase deficiencyOxidation-Reduction
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Papers overview

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1999
1999
Mechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl with the flavin adenine dinucleotide ribityl side chain.
The flavin adenine dinucleotide (FAD) cofactor of pig kidney medium-chain specific acyl-coenzyme A (CoA) dehydrogenase (MCADH… Expand
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1999
1999
Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
Medium-chain acyl-CoA dehydrogenase (MCADH) deficiency, an autosomal recessive inherited disorder, is the most common genetic… Expand
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1998
1998
Substrate activation by acyl-CoA dehydrogenases: transition-state stabilization and pKs of involved functional groups.
The mechanism by which acyl-CoA dehydrogenases initiate catalysis was studied by using p-substituted phenylacetyl-CoAs… Expand
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1997
1997
Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme.
Recombinant, normal human medium-chain acyl-CoA dehydrogenase (MCADH) and the common, human disease-causing K304E mutant ([Glu304… Expand
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Highly Cited
1996
Highly Cited
1996
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active… Expand
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1996
1996
Medium-long-chain chimeric human Acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain Acyl-CoA dehydrogenase.
The catalytically essential glutamate residue that initiates catalysis by abstracting the substrate alpha-hydrogen as H+ is… Expand
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Highly Cited
1990
Highly Cited
1990
Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.
The cDNA of human medium chain acyl-CoA dehydrogenase (MCADH) was modified by in vitro mutagenesis, and the sequence encoding the… Expand
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1990
1990
Selective inactivation of various acyl-CoA dehydrogenases by (methylenecyclopropyl)acetyl-CoA.
Inactivation of five distinct acyl-CoA dehydrogenases by (methylenecyclopropyl)acetyl-CoA (MCPA-CoA), the toxic metabolite of… Expand
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Highly Cited
1987
Highly Cited
1987
Short-chain acyl-coenzyme A dehydrogenase deficiency. Clinical and biochemical studies in two patients.
We describe two patients with short-chain acyl-coenzyme A (CoA) dehydrogenase (SCADH) deficiency. Neonate I excreted large… Expand
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1985
1985
Catalytic defect of medium-chain acyl-coenzyme A dehydrogenase deficiency. Lack of both cofactor responsiveness and biochemical heterogeneity in eight patients.
Medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCADH; EC 1.3.99.3) deficiency (MCD) is an inborn error of beta-oxidation. We… Expand
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