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15 results on '"Ali, Sohail T."'

13. Three-dimensional Structure of a Lipoyl Domain from the Dihydrolipoyl Acetyltransferase Component of the Pyruvate Dehydrogenase Multienzyme Complex ofEscherichia coli

Author

Green, James D. F., Laue, Ernest D., Perham, Richard N., Ali, Sohail T., and Guest, John R.

Abstract

The structure of a lipoyl domain from the pyruvate dehydrogenase multienzyme complex ofEscherichia colihas been determined by means of nuclear magnetic resonance spectroscopy. A total of 549 nuclear Overhauser effect distance restraints, 52 φ torsion angle restraints and 16 slowly exchanging amide protons were employed as input for the structure calculations. These were performed using a combined distance geometry-simulated annealing strategy. The domain is a hybrid between the N and C-terminal halves of the first and third lipoyl domains, respectively, of the dihydrolipoyl acetyltransferase component of theE. colimultienzyme complex, representing residues 1 to 33 and 238 to 289 (wild-type numbering). The lipoyl-lysine residue was also replaced by glutamine. Nonetheless, its structure, two four-stranded β-sheets forming a flattened β-barrel, closely resembles that of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex fromBacillus stearothermophilusdetermined previously. As before, the lipoylation site is physically exposed in a tight turn in one of the β-sheets, and the N and C-terminal residues are close together at the other end of the molecule in adjacent strands of the other β-sheet. Another prominently conserved feature of the structure is the 2-fold axis of quasi-symmetry relating the N and C-terminal halves of the domain. Consistent with the high level of sequence similarity between lipoyl domains of 2-oxo acid dehydrogenase multienzyme complexes from many different sources, these results confirm that all lipoyl domains are likely to have closely related structures.

Published
1995
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14. Genome Sequence of Stenotrophomonas maltophilia PML168, Which Displays Baeyer-Villiger Monooxygenase Activity.

Author

Allen, Michael J., Tait, Karen, Mühling, Martin, Weynberg, Karen, Bradley, Claire, Trivedi, Urmi, Gharbi, Karim, Nissimov, Jozef, Mavromatis, Konstantinos, Jensen, Chantel N., Grogan, Gideon, and Ali, Sohail T.

Subjects
*STENOTROPHOMONAS maltophilia, *BAEYER-Villiger rearrangement, *FLAVOPROTEINS, *GENOMES, *ENZYMES, *MONOOXYGENASES
Abstract

Stenotrophomonas maltophilia PML168 was isolated from Wembury Beach on the English Coast from a rock pool following growth and selection on agar plates. Here we present the permanent draft genome sequence, which has allowed prediction of function for several genes encoding enzymes relevant to industrial biotechnology, including a novel flavoprotein monooxygenase. [ABSTRACT FROM AUTHOR]

Published
2012
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15. Novel targets for antibiotic drug design.

Author

Ali ST, Gill AE, and Lewendon A

Subjects
Animals, Cell Division drug effects, Cell Division physiology, Humans, Anti-Bacterial Agents administration & dosage, Anti-Bacterial Agents chemistry, Drug Delivery Systems methods, Drug Design
Abstract

The urgent need for new antibiotics has led to an explosion in the number and diversity of antibiotic drug targets under investigation. The majority of such targets are enzymes required for essential cellular functions. Often, such novel targets are completely unexploited for antibiotic therapy and therefore have the advantage of avoiding current resistance mechanisms. In general, the most advanced novel targets are drawn from processes where an existing antibacterial compound has validated that process for antibiotic therapy. This review describes a number of the more promising targets under development.

Published
2002

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