EurekaMag
+ Translate
+ Most Popular
Gaucher's disease;thirty-two years experience at Siriraj Hospital
A study of Macrobathra Meyrick from China (Lepidoptera, Cosmopterigidae)
First occurrence in ores of tetragonal chalcocite
Effects of trace element nutrition on sleep patterns in adult women
N.Z. range management guidelines. 2. Design of grazing management systems for tussock country
A case of lipoma of the esophagus
A revision of world Acanthosomatidae (Heteroptera: Pentatomidae): keys to and descriptions of subfamilies, tribes and genera, with designation of types
Life history of the coronate scyphozoan Linuche unguiculata (Swartz, 1788)
Perceptual restoration of obliterated sounds
Mutagenicity studies on two chromium(III) coordination compounds
The formation of the skeleton. I. Growth of a long bone. 1st appearance of a center of calcification
Leucopenia and abnormal liver function in travellers on malaria chemoprophylaxis
The joint commission: four key root causes loom large in sentinel event data
Treatment of vitiligo with topical 15% lactic acid solution in combination with ultra violet-A
Behaviour of dairy cows within three hours after feed supply: I. Influence of housing type and time elapsing after feed supply
Observations of the propagation velocity and formation mechanism of burst fractures caused by gunshot
Management and control of patients with type 2 diabetes mellitus in Lebanon: results from the International Diabetes Management Practices Study (IDMPS)
The diet composition and nutritional knowledge of patients with anorexia nervosa
Physoporella croatica Herak, 1958 of the Slovak karst Anisian (Slovakia, the West Carpathians Mts.)
Bright lights, big noise. How effective are vehicle warning systems?
Ein Plesiosaurier-Rest mit Magensteinen aus mittlerem Lias von Quedlinburg
Incidence of Chlamydia trachomatis in patients with sterility
Monster soup: the microscope and Victorian fantasy
Preliminary tests with residual sprays against poultry lice
Duration of the life of plants in phylogeny

Characterization and conservation of the inner E2 core domain structure of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor


Characterization and conservation of the inner E2 core domain structure of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor



Journal of Biological Chemistry 263(28): 14008-14014



ISSN/ISBN: 0021-9258

PMID: 3049570

A cDNA clone encoding the entire transacylase (E2b) precursor of the bovine branched-chain alpha-keto acid dehydrogenase complex has been constructed from two overlapping incomplete cDNA clones which were isolated from a lambda ZAP library prepared from bovine liver poly(A)+ RNA. Nucleotide sequencing indicates that this bovine E2b cDNA insert (bE2-11) is 2701 base pairs in length with an open reading frame of 1446 base pairs. The bE2-11 cDNA insert encodes a leader peptide of 61 residues and a mature E2b polypeptide of 421 amino acid residues with a calculated monomeric molecular mass of 46,518 daltons. The molecular mass of the native E2b component isolated from bovine liver is 1,110,000 daltons as determined by sedimentation equilibrium. This value establishes the 24-subunit octahedral model for the quaternary structure of bovine E2b. The amino-terminal sequences of two tryptic fragments (A and B) of the E2b protein have been determined. Fragment A comprises residues 175 to 421 of the E2b protein and is the inner E2 core domain which contains the transacylase active site. Fragment B, produced by further tryptic cleavage of fragment, comprises residues 205 to 421, but does not have transacylase activity. Both fragments A and B confer the highly assembled 24-mer structure. The primary structure of the inner E2 core domain of bovine E2b (fragment A) is very similar to those of three other E2 proteins (human E2p, Escherichia coli E2p, and E. coli E2k). These similarities suggest that these E2 proteins are structurally and evolutionarily related.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 039517701

Download citation: RISBibTeXText

Related references

Characterization and conservation of the inner E2 core domain structure of branched-chain a-keto acid dehydrogenase complex from bovine liver. Construction of a cDNA encoding the entire transacylase (E2b) precursor. The Journal of Biological Chemistry 263: 008-14, 1988

Characterization and conservation of the inner E2 core domain structure of branched-chain α-keto acid dehydrogenase complex from bovine liver: construction of a cDNA encoding the entire transacylase (E2b) precursor. The Journal of Biological Chemistry 263(28): 14008-14014, 1988

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

Characterization and conservation of the inner e 2 core domain structure of the bovine branched chain alpha keto acid dehydrogenase complex. Roche, T E And M S Patel (Ed ) Annals Of The New York Academy Of Sciences, Vol 573 Alpha-Keto Acid Dehydrogenase Complexes: Organization, Regulation, And Biomedical Ramifications: A Tribute to Lester J Reed; Conference, Austin, Texas, Usa, November 16-18, 1988 Xviii+474p New York Academy Of Sciences: New York, New York, Usa Illus Maps 432-434, 1989

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 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 alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry 27(6): 1972-1981, 1988

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 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

Isolation and sequencing of a cDNA encoding the decarboxylase (E1)alpha precursor of bovine branched-chain alpha-keto acid dehydrogenase complex. Expression of E1 alpha mRNA and subunit in maple-syrup-urine-disease and 3T3-L1 cells. Journal of Biological Chemistry 263(18): 9007-9014, 1988

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

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 a-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. Biochemistry (American Chemical Society) 27: 72-80, 1988