Kinetic, spectral, and structural studies of the slow-binding inhibition of the Escherichia coli dihydrodipicolinate synthase by 2, 4-oxo-pentanoic acid

2021 ◽  
Vol 702 ◽  
pp. 108819
Author(s):  
William Karsten ◽  
Leonard M. Thomas ◽  
Christian Fleming ◽  
Priscilla Seabourn ◽  
Christina Bruxvoort ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Studies ◽  
Dihydrodipicolinate Synthase ◽  
Pentanoic Acid ◽  
Binding Inhibition

scholarly journals Structural studies of the membrane-derived oligosaccharides of Escherichia coli.

1979 ◽  
Vol 254 (20) ◽  
pp. 10135-10138
Author(s):  
J.E. Schneider ◽  
V. Reinhold ◽  
M.K. Rumley ◽  
E.P. Kennedy
Keyword(s):  
Escherichia Coli ◽  
Structural Studies

Structural studies of the Escherichia coli O-antigen 25

1983 ◽  
Vol 122 (2) ◽  
pp. 249-256 ◽  
Author(s):  
Lennart Kenne ◽  
Bengt Lindberg ◽  
John K. Madden ◽  
Alf A. Lindberg ◽  
Peter Gemski
Keyword(s):  
Escherichia Coli ◽  
Structural Studies ◽  
O Antigen

Structural studies of the Escherichia coli O1A O-polysaccharide, using the computer program CASPER

1991 ◽  
Vol 211 (1) ◽  
pp. 183-190 ◽  
Author(s):  
Herbert Baumann ◽  
Per-Erik Jansson ◽  
Lennart Kenne ◽  
Göran Widmalm
Keyword(s):  
Escherichia Coli ◽  
Computer Program ◽  
Structural Studies

scholarly journals Two-dimensional crystallization of Escherichia coli-expressed bacteriorhodopsin and its D96N variant: high resolution structural studies in projection

1993 ◽  
Vol 65 (3) ◽  
pp. 1295-1306 ◽  
Author(s):  
A.K. Mitra ◽  
L.J. Miercke ◽  
G.J. Turner ◽  
R.F. Shand ◽  
M.C. Betlach ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Resolution ◽  
Two Dimensional ◽  
Structural Studies

scholarly journals Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2 component of the human pyruvate dehydrogenase complex

1993 ◽  
Vol 289 (1) ◽  
pp. 81-85 ◽  
Author(s):  
J Quinn ◽  
A G Diamond ◽  
A K Masters ◽  
D E Brookfield ◽  
N G Wallis ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Structural Studies ◽  
Gene Encoding ◽  
E Coli ◽  
Inner Lipoyl Domain ◽  
Dehydrogenase Complex ◽  
Lipoyl Domain

The dihydrolipoamide acetyltransferase subunit (E2p) of mammalian pyruvate dehydrogenase complex has two highly conserved lipoyl domains each modified with a lipoyl cofactor bound in amide linkage to a specific lysine residue. A sub-gene encoding the inner lipoyl domain of human E2p has been over-expressed in Escherichia coli. Two forms of the domain have been purified, corresponding to lipoylated and non-lipoylated species. The apo-domain can be lipoylated in vitro with partially purified E. coli lipoate protein ligase, and the lipoylated domain can be reductively acetylated by human E1p (pyruvate dehydrogenase). Availability of the two forms will now allow detailed biochemical and structural studies of the human lipoyl domains.

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