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The three-dimensional structure of shikimate kinase.

Journal of molecular biology, 1998
The three-dimensional structure of shikimate kinase from Erwinia chrysanthemi has been determined by multiple isomorphous replacement. Two models are presented: a high resolution 1.9 A model and a 2.6 A model which contains bound Mg-ADP. The enzyme is an alpha/beta protein consisting of a central sheet of five parallel beta-strands flanked by alpha ...
T, Krell, J R, Coggins, A J, Lapthorn
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Effects of salts on the function and conformational stability of shikimate kinase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The unfolding of shikimate kinase (SK) from Erwinia chrysanthemi by urea and its subsequent refolding on dilution of the denaturing agent has been studied in detail [Eur. J. Biochem. 269 (2002) 2124]. Comparison of the effects of urea on the enzyme with those of guanidinium chloride (GdmCl) and NaCl indicated that chloride ions significantly weakened ...
Eleonora, Cerasoli   +5 more
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Crystal Structure of Mycobacterium tuberculosis Shikimate Kinase in Complex with Shikimic Acid and an ATP Analogue,

Biochemistry, 2006
Shikimate kinase (SK) and other enzymes in the shikimate pathway are potential targets for developing nontoxic antimicrobial agents, herbicides, and antiparasite drugs, because the pathway is essential in microorganisms, plants, and parasites but absent from mammals. SK catalyzes the reaction of phosphoryl transfer from ATP to shikimic acid (SA). Since
Jianhua, Gan   +4 more
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Interaction of shikimic acid with shikimate kinase.

Biochemical and biophysical research communications, 2005
The crystal structure of shikimate kinase from Mycobacterium tuberculosis (MtSK) complexed with MgADP and shikimic acid (shikimate) has been determined at 2.3A resolution, clearly revealing the amino acid residues involved in shikimate binding. In MtSK, the Glu61 strictly conserved in SK forms a hydrogen bond and salt-bridge with Arg58 and assists in ...
José Henrique, Pereira   +7 more
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Shikimate Kinase: A Potential Target for Development of Novel Antitubercular Agents

Current Drug Targets, 2007
Tuberculosis (TB) remains the leading cause of mortality due to a bacterial pathogen, Mycobacterium tuberculosis. However, no new classes of drugs for TB have been developed in the past 30 years. Therefore there is an urgent need to develop faster acting and effective new antitubercular agents, preferably belonging to new structural classes, to better ...
José H, Pereira   +6 more
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Folding and stability of shikimate kinase

2002
Shikimate kinase (SK; EC 2.7.1.71), an enzyme that catalyses the specific phosphorylation of the 3-hydroxyl group of shikimate using ATP as the phosphoryl donor, was chosen as a representative example of a subclass of a/p proteins with which to examine the unfolding, stability and mechanism of protein folding.
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Mechanism of Phosphoryl Transfer Catalyzed by Shikimate Kinase from Mycobacterium tuberculosis

Journal of Molecular Biology, 2006
The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by ...
Hartmann, M. ; https://orcid.org/0000-0001-6937-5677   +4 more
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Structure and stability studies of shikimate kinase

1999
This thesis describes a structural and functional study of shikimate kinase, the enzyme which catalyses the fifth step in the biosynthetic shikimate pathway in which shikimate is converted to shikimate-3 -phosphate. Mutagenesis studies were undertaken to discover more about the roles of the assumed catalytic residues in particular the single lysine ...
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Stimulation by thioredoxin of shikimate kinase from spinach chloroplasts

Physiologia Plantarum, 1987
The activity of shikimate kinase (EC 2.7.1.71) from spinach (Spinacia oleracea L.) chloroplasts was increased up to 8.5‐fold by addition of thioredoxin and dithio‐threitol.
C. L. Schmidt, G. Schultz
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In silico characterization of Shikimate Kinase of Shigella flexneri: A potential drug target

Interdisciplinary Sciences: Computational Life Sciences, 2010
Shigella flexneri is a major pathogen responsible for Shigellosis causing massive morbidity among young population and imposes huge socio-economic burden. In this study, Shikimate Kinase (SK) from S. flexneri was characterized in silico and disordered regions were predicted. Motifs and domains were calculated using computational tools.
Neelima, Arora   +2 more
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