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Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain a-keto acid dehydrogenase


Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain a-keto acid dehydrogenase



The Journal of Biological Chemistry 259: 77-84




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Related references

Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase. The Journal of Biological Chemistry 259(14): 9277-9284, 1984

Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid dehydrogenase. Journal of Biological Chemistry 259(14): 9277-9284, 1984

Subunit structure of the dihydrolipoyl transacylase component of branched-chain a-keto acid dehydrogenase complex from bovine liver. Characterization of the inner transacylase core. The Journal of Biological Chemistry 260: 779-86, 1985

Subunit structure of the dihydrolipoyl transacylase component of branched-chain α-keto acid dehydrogenase complex from bovine liver: characterization of the inner transacylase core. The Journal of Biological Chemistry 260(25): 13779-13786, 1985

Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Characterization of the inner transacylase core. Journal of Biological Chemistry 260(25): 13779-13786, 1985

Subunit structure of the dihydrolipoyl transacylase component of branched-chain α-keto acid dehydrogenase complex from bovine liver: mapping of the lipoyl-bearing domain by limited proteolysis. The Journal of Biological Chemistry 261(1): 343-349, 1986

Subunit structure of the dihydrolipoyl transacylase component of branched-chain a-keto acid dehydrogenase complex from bovine liver. Mapping of the lipoyl-bearing domain by limited proteolysis. The Journal of Biological Chemistry 261: 3-9, 1986

Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Mapping of the lipoyl-bearing domain by limited proteolysis. Journal of Biological Chemistry 261(1): 343-349, 1986

Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain a-keto acid dehydrogenase complex and characterization of an E2 pseudogene. The Journal of Biological Chemistry 267: 090-6, 1992

Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. Journal of Biological Chemistry 267(33): 24090-24096, 1992

Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain a-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry (American Chemical Society) 27: 72-80, 1988

Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain α-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry (Easton) 27(6): 1972-1981, 1988

Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry 27(6): 1972-1981, 1988

Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex. Molecular Biology and Medicine 8(1): 49-63, 1991

Identification of mutations in the dihydrolipoyl transacylase e2 subunit of the branched chain alpha keto acid dehydrogenase complex. FASEB Journal 5(5): A1199, 1991