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| {{STRUCTURE_1uk8| PDB=1uk8 | SCENE= }} | | {{STRUCTURE_1uk8| PDB=1uk8 | SCENE= }} |
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| '''Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate'''
| | ===Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with n-valerate=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15784976}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15784976 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15784976}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pseudomonas fluorescens ip01]] | | [[Category: Pseudomonas fluorescens ip01]] |
| [[Category: Substrate specificity]] | | [[Category: Substrate specificity]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:20:33 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:59:56 2008'' |
