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2v29
From Proteopedia
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[[Image:2v29.png|left|200px]] | [[Image:2v29.png|left|200px]] | ||
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{{STRUCTURE_2v29| PDB=2v29 | SCENE= }} | {{STRUCTURE_2v29| PDB=2v29 | SCENE= }} | ||
===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)=== | ===L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)=== | ||
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==See Also== | ==See Also== | ||
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Revision as of 17:37, 25 July 2012
Contents |
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)
Template:ABSTRACT PUBMED 18085797
About this Structure
2v29 is a 2 chain structure of Aldolase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Grueninger D, Schulz GE. Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2008 Jan 15;47(2):607-14. Epub 2007 Dec 18. PMID:18085797 doi:http://dx.doi.org/10.1021/bi7012799
- Kroemer M, Merkel I, Schulz GE. Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:12962479 doi:http://dx.doi.org/10.1021/bi0349266
Categories: Escherichia coli | Rhamnulose-1-phosphate aldolase | Grueninger, D. | Schulz, G E. | 2-ketose degradation | Aldolase | Bacterial l-rhamnose metabolism | Class ii | Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone phosphate | Domain motion for mechanical support of catalysis | Lyase | Metal-binding | Protein engineering | Protein-protein interface | Rare sugar | Rhamnose metabolism | Surface mutation | Zinc enzyme
