The Interaction Between Lipoamide Dehydrogenase and the Peripheral‐Component‐Binding Domain from the Azotobacter Vinelandii Pyruvate Dehydrogenase Complex

European Journal of Biochemistry

Volumn 234, Issue 3, 1995, Pages 861-870

  Westphal, Adrie H ^a   Fabisz‐Kijowska, Anna ^a   Kester, Henri ^a   Obels, Peter P ^a   De Kok, Aart ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

binding domain; interaction; lipoamide dehydrogenase; pyruvate dehydrogenase complex

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; MULTIENZYME COMPLEX; OXIDOREDUCTASE;

ARTICLE; AZOTOBACTER VINELANDII; BINDING SITE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INHIBITION; MOLECULAR CLONING; MUTANT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN DOMAIN; SPECTROSCOPY;

AMINO ACID SEQUENCE; AZOTOBACTER VINELANDII; BINDING SITES; CHYMOTRYPSIN; DIHYDROLIPOAMIDE DEHYDROGENASE; ESCHERICHIA COLI; EXONUCLEASES; KETOGLUTARATE DEHYDROGENASE COMPLEX; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; NAD; PROTEIN BINDING; PROTEIN CONFORMATION; PYRUVATE DEHYDROGENASE COMPLEX; RECOMBINANT FUSION PROTEINS; SPECTROPHOTOMETRY;

EID: 0029586365     PISSN: 00142956     EISSN: 14321033     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1995.861_a.x     Document Type: Article

References (40)

1. Lipoamide dehydrogenase from Azotobacter vinelandii: site‐directed mutagenesis of the His450‐Glu455 diad. Spectral properties of wild‐type and mutated enzymes
2. Lipoamide dehydrogenase from Azotobacter vinelandii, The role of the C‐terminus in catalysis and dimer stabilization
3. Lipoamide dehydrogenase from Azotobacter vinelandii: site‐directed mutagenesis of the His450‐Glu455 diad. Kinetics of wild‐type and mutated enzymes
4. Assays of proteins in the presence of interfering materials
5. Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N‐terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
6. The composition of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Does a unifying model exist for the complexes from gram‐negative bacteria?
7. The three‐dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
8. Hybrid pyruvate dehydrogenase complexes reconstituted from components of the complexes from Escherichia coli and Azotobacter vinelandii
9. The pyruvate dehydrogenase complex from Azotobacter vinelandii
10. A microbiuret method for protein determination of total protein in cerebrospinal fluid
11. The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
12. The gene encoding dihydrolipoyl transacetylase from Azotobacter vinelandii. Expression in Escherichia coli and activation and isolation of the protein
13. The high resolution structure of the peripheral subunit‐binding domain of dihydralipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus
14. The refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution
15. The pyruvate dehydrogenase multienzyme complex
16. + at 2.45 Å resolution
17. The atomic structure of the cubic core of the pyruvate dehydrogenase complex
18. The refined crystal structure of Pseudomonas fluorescens lipoamide dehydrogenase at 2.8 Å resolution: analysis of redox and thermostability properties
19. Measurement of the oxidation‐reduction potentials for two‐electron and four‐electron reduction of lipoamide dehydrogenase from pig heart
20. 2‐Oxo acid dehydrogenase multienzyme complexes: domains, dynamics and design
21. Studies on the kinetic mechanism of lipoamide dehydrogenase from rat liver mitochondria
22. Multienzyme complexes
23. Three‐dimensional solution structure of the E3‐binding domain of the dihydrolipoamide transsuccinylase core from the 2‐oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
24. Lipoamide dehydrogenase from Escherichia
25. Tricine‐sodium dodecyl sulphate polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
26. Dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12
27. Site‐directed mutagenesis of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii
28. Interaction of lipoamide dehydrogenase with the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
29. Reconstitution of pyruvate dehydrogenase multienzyme complexes based on chimeric core structures from Azotobacter vinelandii and Escherichia coli
30. Structure/function relationships in the pyruvate. dehydrogenase complex from Azotobacter vinelandii. Role of the linker region between the binding and catalytic domain of the dihydrolipoyl transacetylase component
31. Alpha‐keto acid dehydrogenase complexes. XII. Effects of acetylation on the activity and structure of the dihydrolipoyl transacetylase of Escherichia
32. Differences in sensitivity to NADH of purified pyruvate dehydrogenase complexes from Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli: implications for their activity in vivo
33. The conformational stability of the redox states of liponmide dehydrogenase from Azotobacter vinelandii
34. Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene
35. The 2‐oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component
36. Evidence for multiple electronic forms of two‐electron reduced lipoamide dehydrogenase from Escherichia coli
37. + activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH‐lipoamide reaction
38. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase and mercuric reductase‐family of flavoenzyme transhydrogenases