9ldb: Difference between revisions
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[[Image:9ldb.gif|left|200px]] | [[Image:9ldb.gif|left|200px]] | ||
'''DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK''' | {{Structure | ||
|PDB= 9ldb |SIZE=350|CAPTION= <scene name='initialview01'>9ldb</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=OXM:OXAMIC ACID'>OXM</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] | |||
|GENE= | |||
}} | |||
'''DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
9LDB is a [ | 9LDB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LDB OCA]. | ||
==Reference== | ==Reference== | ||
Design and synthesis of new enzymes based on the lactate dehydrogenase framework., Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ, Philos Trans R Soc Lond B Biol Sci. 1991 May 29;332(1263):177-84. PMID:[http:// | Design and synthesis of new enzymes based on the lactate dehydrogenase framework., Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ, Philos Trans R Soc Lond B Biol Sci. 1991 May 29;332(1263):177-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1678537 1678537] | ||
[[Category: L-lactate dehydrogenase]] | [[Category: L-lactate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase(choh(d)-nad+(a))]] | [[Category: oxidoreductase(choh(d)-nad+(a))]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:16:36 2008'' | ||
Revision as of 20:16, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | , , and | ||||||
| Activity: | L-lactate dehydrogenase, with EC number 1.1.1.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DESIGN AND SYNTHESIS OF NEW ENZYMES BASED ON THE LACTATE DEHYDROGENASE FRAMEWORK
OverviewOverview
Analysis of the mechanism and structure of lactate dehydrogenases is summarized in a map of the catalytic pathway. Chemical probes, single tryptophan residues inserted at specific sites and a crystal structure reveal slow movements of the protein framework that discriminate between closely related small substrates. Only small and correctly charged substrates allow the protein to engulf the substrate in an internal vacuole that is isolated from solvent protons, in which water is frozen and hydride transfer is rapid. The closed vacuole is very sensitive to the size and charge of the substrate and provides discrimination between small substrates that otherwise have too few functional groups to be distinguished at a solvated protein surface. This model was tested against its ability to successfully predict the design and synthesis of new enzymes such as L-hydroxyisocaproate dehydrogenase and fully active malate dehydrogenase. Solvent friction limits the rate of forming the vacuole and thus the maximum rate of catalysis.
About this StructureAbout this Structure
9LDB is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Design and synthesis of new enzymes based on the lactate dehydrogenase framework., Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ, Philos Trans R Soc Lond B Biol Sci. 1991 May 29;332(1263):177-84. PMID:1678537
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