1uk9
From Proteopedia
(New page: 200px<br /><applet load="1uk9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uk9, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1uk9.jpg|left|200px]]<br /><applet load="1uk9" size=" | + | [[Image:1uk9.jpg|left|200px]]<br /><applet load="1uk9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uk9, resolution 1.80Å" /> | caption="1uk9, resolution 1.80Å" /> | ||
'''Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with isovalerate'''<br /> | '''Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with isovalerate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Meta-cleavage product hydrolase (MCP-hydrolase) is one of the key enzymes | + | 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== | ==About this Structure== | ||
| - | 1UK9 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 IVA 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:// | + | 1UK9 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=IVA:'>IVA</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=1UK9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fushinobu, S.]] | [[Category: Fushinobu, S.]] | ||
[[Category: Hidaka, M.]] | [[Category: Hidaka, M.]] | ||
| - | [[Category: Jun, S | + | [[Category: Jun, S Y.]] |
[[Category: Nojiri, H.]] | [[Category: Nojiri, H.]] | ||
[[Category: Omori, T.]] | [[Category: Omori, T.]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:34 2008'' |
Revision as of 13:25, 21 February 2008
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Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with isovalerate
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
1UK9 is a Single protein structure of sequence from Pseudomonas fluorescens with as ligand. Active as 2-hydroxymuconate-semialdehyde hydrolase, with EC number 3.7.1.9 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 Feb 21 15:25:34 2008
Categories: 2-hydroxymuconate-semialdehyde hydrolase | Pseudomonas fluorescens | Single protein | Fushinobu, S. | Hidaka, M. | Jun, S Y. | Nojiri, H. | Omori, T. | Shoun, H. | Wakagi, T. | Yamane, H. | IVA | Alpha/beta-hydrolase | Aromatic compounds | Beta-ketolase | Cumene | Cumene degradation | Isopropylbenzene | Meta-cleavage compound hydrolase | Pcb | Polychlorinated biphenyl degradation | Pseudomonas fluorescens ip01 | Substrate specificity
