1dzu
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Previous analyses established the structures of unligated L-fuculose | + | Previous analyses established the structures of unligated L-fuculose 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking the substrate dihydroxyacetone phosphate. These data allowed us to suggest a catalytic mechanism. On the basis of this proposal, numerous mutations were now introduced at the active center and tested with respect to their catalytic rates and their product distributions. For several mutants, the structures were determined. The results demonstrate the catalytic importance of some particular residues in defined conformations and in the mobile C-terminal chain end. Moreover, they led to a modification of the proposed mechanism. The effect of some mutations on enantioselectivity and on the ratio of diastereomer formation indicates clearly the binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate. |
==About this Structure== | ==About this Structure== | ||
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[[Category: L-fuculose-phosphate aldolase]] | [[Category: L-fuculose-phosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Joerger, A | + | [[Category: Joerger, A C.]] |
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: mutant structure]] | [[Category: mutant structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:17 2008'' |
Revision as of 10:22, 21 February 2008
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L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT T26A
Overview
Previous analyses established the structures of unligated L-fuculose 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking the substrate dihydroxyacetone phosphate. These data allowed us to suggest a catalytic mechanism. On the basis of this proposal, numerous mutations were now introduced at the active center and tested with respect to their catalytic rates and their product distributions. For several mutants, the structures were determined. The results demonstrate the catalytic importance of some particular residues in defined conformations and in the mobile C-terminal chain end. Moreover, they led to a modification of the proposed mechanism. The effect of some mutations on enantioselectivity and on the ratio of diastereomer formation indicates clearly the binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
About this Structure
1DZU is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis., Joerger AC, Gosse C, Fessner WD, Schulz GE, Biochemistry. 2000 May 23;39(20):6033-41. PMID:10821675
Page seeded by OCA on Thu Feb 21 12:22:17 2008
