1hm4

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|SITE=
|SITE=
|LIGAND=
|LIGAND=
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|RELATEDENTRY=[[1hm7|1HM7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hm4 OCA], [http://www.ebi.ac.uk/pdbsum/1hm4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hm4 RCSB]</span>
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[[Category: terpene]]
[[Category: terpene]]
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Revision as of 18:07, 30 March 2008


PDB ID 1hm4

Drag the structure with the mouse to rotate
, resolution 3.47Å
Activity: Pentalenene synthase, with EC number 4.2.3.7
Related: 1HM7


Resources: FirstGlance, OCA, PDBsum, RCSB
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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