de Kok A - Search Results

1

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.

Berg A, de Kok A, Vervoort J. Berg A, et al. Among authors: de kok a. Eur J Biochem. 1994 Apr 1;221(1):87-100. doi: 10.1111/j.1432-1033.1994.tb18717.x. Eur J Biochem. 1994. PMID: 8068086 Free article.

2

Time-resolved fluorescence studies on mutants of the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii.

Schulze E, Westphal AH, Berg A, de Kok A. Schulze E, et al. Among authors: de kok a. FEBS Lett. 1990 Oct 29;273(1-2):46-50. doi: 10.1016/0014-5793(90)81047-r. FEBS Lett. 1990. PMID: 2226864 Free article.

3

The gene encoding dihydrolipoyl transacetylase from Azotobacter vinelandii. Expression in Escherichia coli and activation and isolation of the protein.

Hanemaaijer R, Westphal AH, Berg A, Van Dongen W, de Kok A, Veeger C. Hanemaaijer R, et al. Among authors: de kok a. Eur J Biochem. 1989 Apr 15;181(1):47-53. doi: 10.1111/j.1432-1033.1989.tb14692.x. Eur J Biochem. 1989. PMID: 2653824 Free article.

4

Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy.

Hanemaaijer R, Vervoort J, Westphal AH, de Kok A, Veeger C. Hanemaaijer R, et al. Among authors: de kok a. FEBS Lett. 1988 Nov 21;240(1-2):205-10. doi: 10.1016/0014-5793(88)80369-7. FEBS Lett. 1988. PMID: 3191993 Free article.

5

Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for high structural similarity with the lipoyl domain of the pyruvate dehydrogenase complex.

Berg A, Smits O, de Kok A, Vervoort J. Berg A, et al. Among authors: de kok a. Eur J Biochem. 1995 Nov 15;234(1):148-59. doi: 10.1111/j.1432-1033.1995.148_c.x. Eur J Biochem. 1995. PMID: 8529634 Free article.

6

Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii.

Berg A, Vervoort J, de Kok A. Berg A, et al. Among authors: de kok a. J Mol Biol. 1996 Aug 23;261(3):432-42. doi: 10.1006/jmbi.1996.0474. J Mol Biol. 1996. PMID: 8780784

7

Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.

Berg A, Vervoort J, de Kok A. Berg A, et al. Among authors: de kok a. Eur J Biochem. 1997 Mar 1;244(2):352-60. doi: 10.1111/j.1432-1033.1997.00352.x. Eur J Biochem. 1997. PMID: 9119000 Free article.

8

Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii.

Berg A, Westphal AH, Bosma HJ, de Kok A. Berg A, et al. Among authors: de kok a. Eur J Biochem. 1998 Feb 15;252(1):45-50. doi: 10.1046/j.1432-1327.1998.2520045.x. Eur J Biochem. 1998. PMID: 9523710 Free article.

9

Reconstitution of pyruvate dehydrogenase multienzyme complexes based on chimeric core structures from Azotobacter vinelandii and Escherichia coli.

Schulze E, Westphal AH, Veeger C, de Kok A. Schulze E, et al. Among authors: de kok a. Eur J Biochem. 1992 Jun 1;206(2):427-35. doi: 10.1111/j.1432-1033.1992.tb16943.x. Eur J Biochem. 1992. PMID: 1597183 Free article.

A. vinelandii E3 interacts only with those chimeras that contain the A. vinelandii binding domain, whereas E. coli E3 interacts with all chimeras. ...These observations confirm previous conclusions, based on site-directed mutagenesis of A. vinelandii E2p [Sch …

A. vinelandii E3 interacts only with those chimeras that contain the A. vinelandii binding domain, whereas E. coli E3 interact …

10

Site-directed mutagenesis of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.

Schulze E, Westphal AH, Boumans H, de Kok A. Schulze E, et al. Among authors: de kok a. Eur J Biochem. 1991 Dec 18;202(3):841-8. doi: 10.1111/j.1432-1033.1991.tb16441.x. Eur J Biochem. 1991. PMID: 1765097 Free article.

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