2d0d

Revision as of 19:52, 29 January 2008 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2d0d" size="350" color="white" frame="true" align="right" spinBox="true" caption="2d0d, resolution 1.65Å" /> '''Crystal Structure of...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)

Crystal Structure of a Meta-cleavage Product Hydrolase (CumD) A129V Mutant

File:2d0d.gif


2d0d, resolution 1.65Å

Drag the structure with the mouse to rotate

OverviewOverview

The meta-cleavage product hydrolase from Pseudomonas fluorescens IP01, (CumD) hydrolyzes 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate (6-isopropyl, HODA) in the cumene (isopropylbenzene) degradation pathway. To modulate, the substrate specificity and catalytic efficiency of CumD toward, substrates derived from monocyclic aromatic compounds, we constructed the, CumD mutants, A129V, I199V, and V227I, as well as four types of double and, triple mutants. Toward substrates with smaller side chains (e.g., 2-hydroxy-6-oxohepta-2,4-dienoate; 6-ethyl-HODA), the k(cat)/K(m) values, of the single mutants were 4.2-11 fold higher than that of the wild type, enzyme and 1.8-4.7 fold higher than that of the meta-cleavage product, hydrolase from Pseudomonas putida F1 (TodF). The A129V mutant showed the, highest k(cat)/K(m) value for 2-hydroxy-6-oxohepta-2,4-dienoate, (6-ethyl-HODA). The crystal structure of the A129V mutant was determined, at 1.65 A resolution, enabling location of the Ogamma atom of the Ser103, side chain. A chloride ion was bound to the oxyanion hole of the active, site, and mutant enzymes at the residues forming this site were also, examined. The k(cat) values of Ser34 mutants were decreased 2.9-65 fold, suggesting that the side chain of Ser34 supports catalysis by stabilizing, the anionic oxygen of the proposed intermediate state (gem-diolate). This, is the first crystal structure determination of CumD in an active form, with the Ser103 residue, one of the catalytically essential "triad", being, intact.

About this StructureAbout this Structure

2D0D is a Single protein structure of sequence from Pseudomonas fluorescens with and as ligands. Active as 2-hydroxymuconate-semialdehyde hydrolase, with EC number 3.7.1.9 Full crystallographic information is available from OCA.

ReferenceReference

Improving the catalytic efficiency of a meta-cleavage product hydrolase (CumD) from Pseudomonas fluorescens IP01., Jun SY, Fushinobu S, Nojiri H, Omori T, Shoun H, Wakagi T, Biochim Biophys Acta. 2006 Jul;1764(7):1159-66. Epub 2006 Jun 7. PMID:16844437

Page seeded by OCA on Tue Jan 29 18:52:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA