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1uk8

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[[Image:1uk8.jpg|left|200px]]<br /><applet load="1uk8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uk8.jpg|left|200px]]
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caption="1uk8, resolution 1.60&Aring;" />
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'''Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate'''<br />
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{{Structure
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|PDB= 1uk8 |SIZE=350|CAPTION= <scene name='initialview01'>1uk8</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=LEA:LEVULINIC ACID'>LEA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/2-hydroxymuconate-semialdehyde_hydrolase 2-hydroxymuconate-semialdehyde hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.9 3.7.1.9]
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|GENE= CUMD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 Pseudomonas fluorescens])
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}}
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'''Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with <scene name='pdbligand=LEA:'>LEA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-hydroxymuconate-semialdehyde_hydrolase 2-hydroxymuconate-semialdehyde hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.9 3.7.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK8 OCA].
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1UK8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK8 OCA].
==Reference==
==Reference==
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A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products., Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Biosci Biotechnol Biochem. 2005 Mar;69(3):491-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15784976 15784976]
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A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products., Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Biosci Biotechnol Biochem. 2005 Mar;69(3):491-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15784976 15784976]
[[Category: 2-hydroxymuconate-semialdehyde hydrolase]]
[[Category: 2-hydroxymuconate-semialdehyde hydrolase]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: LEA]]
[[Category: LEA]]
[[Category: alpha/beta-hydrolase]]
[[Category: alpha/beta-hydrolase]]
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[[Category: aromatic compounds]]
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[[Category: aromatic compound]]
[[Category: beta-ketolase]]
[[Category: beta-ketolase]]
[[Category: cumene]]
[[Category: cumene]]
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[[Category: substrate specificity]]
[[Category: substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:02 2008''

Revision as of 12:33, 20 March 2008

Image:1uk8.jpg


PDB ID 1uk8

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands:
Gene: CUMD (Pseudomonas fluorescens)
Activity: 2-hydroxymuconate-semialdehyde hydrolase, with EC number 3.7.1.9
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate


Overview

Meta-cleavage product hydrolase (MCP-hydrolase) is one of the key enzymes in the microbial degradation of aromatic compounds. MCP-hydrolase produces 2-hydroxypenta-2,4-dienoate and various organic acids, according to the C6 substituent of the substrate. Comprehensive analysis of the substrate specificity of the MCP-hydrolase from Pseudomonas fluorescens IP01 (CumD) was carried out by determining the kinetic parameters for nine substrates and crystal structures complexed with eight cleavage products. CumD preferred substrates with long non-branched C6 substituents, but did not effectively hydrolyze a substrate with a phenyl group. Superimposition of the complex structures indicated that benzoate was bound in a significantly different direction than other aliphatic cleavage products. The directions of the bound organic acids appeared to be related with the k(cat) values of the corresponding substrates. The Ile139 and Trp143 residues on helix alpha4 appeared to cause steric hindrance with the aromatic ring of the substrate, which hampers base-catalyzed attack by water.

About this Structure

1UK8 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products., Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T, Biosci Biotechnol Biochem. 2005 Mar;69(3):491-8. PMID:15784976

Page seeded by OCA on Thu Mar 20 14:33:02 2008

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