2v29
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
- | [[2v29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V29 OCA]. | + | [[2v29]] is a 2 chain structure of [[Aldolase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V29 OCA]. |
+ | |||
+ | ==See Also== | ||
+ | *[[Aldolase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018085797</ref><ref group="xtra">PMID:012962479</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rhamnulose-1-phosphate aldolase]] | [[Category: Rhamnulose-1-phosphate aldolase]] | ||
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[[Category: Rhamnose metabolism]] | [[Category: Rhamnose metabolism]] | ||
[[Category: Surface mutation]] | [[Category: Surface mutation]] | ||
- | [[Category: Zinc]] | ||
[[Category: Zinc enzyme]] | [[Category: Zinc enzyme]] |
Revision as of 05:50, 24 August 2011
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