1hm4
From Proteopedia
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| - | [[Image:1hm4.gif|left|200px]] | + | [[Image:1hm4.gif|left|200px]] |
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| - | '''N219L PENTALENENE SYNTHASE''' | + | {{Structure |
| + | |PDB= 1hm4 |SIZE=350|CAPTION= <scene name='initialview01'>1hm4</scene>, resolution 3.47Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Pentalenene_synthase Pentalenene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.7 4.2.3.7] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''N219L PENTALENENE SYNTHASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HM4 is a [ | + | 1HM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM4 OCA]. |
==Reference== | ==Reference== | ||
| - | Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis., Seemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE, J Am Chem Soc. 2002 Jul 3;124(26):7681-9. PMID:[http:// | + | Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis., Seemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE, J Am Chem Soc. 2002 Jul 3;124(26):7681-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12083921 12083921] |
[[Category: Pentalenene synthase]] | [[Category: Pentalenene synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: terpene]] | [[Category: terpene]] | ||
| - | ''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 11:38:51 2008'' |
Revision as of 09:38, 20 March 2008
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| , resolution 3.47Å | |||||||
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| Activity: | Pentalenene synthase, with EC number 4.2.3.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N219L PENTALENENE SYNTHASE
Overview
Incubation of farnesyl diphosphate (1) with the W308F or W308F/H309F mutants of pentalenene synthase, an enzyme from Streptomyces UC5319, yielded pentalenene (2), accompanied by varying proportions of (+)-germacrene A (7) with relatively minor changes in k(cat) and k(cat)/K(m). By contrast, single H309 mutants gave rise to both (+)-germacrene A (7) and protoilludene (8) in addition to pentalenene (2). Mutation to glutamate of each of the three aspartate residues in the Mg(2+)-binding aspartate-rich domain, (80)DDLFD, resulted in reduction in the k(cat)/K(m) for farnesyl diphosphate and formation of varying proportions of pentalenene and (+)-germacrene A (7). Formation of (+)-germacrene A (7) by the various pentalenene synthase mutants is the result of a derailment of the natural anti-Markovnikov cyclization reaction, and not simply the consequence of trapping of a normally cryptic, carbocationic intermediate. Both the N219A and N219L mutants of pentalenene synthase were completely inactive, while the corresponding N219D mutant had a k(cat)/K(m) which was 3300-fold lower than that of the wild-type synthase, and produced a mixture of pentalenene (2) (91%) and the aberrant cyclization product beta-caryophyllene (9) (9%). Finally, the F77Y mutant had a k(cat)/K(m) which was reduced by 20-fold compared to that of the wild-type synthase.
About this Structure
1HM4 is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.
Reference
Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis., Seemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE, J Am Chem Soc. 2002 Jul 3;124(26):7681-9. PMID:12083921
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