1UK7: Crystal Structure Of A Meta-Cleavage Product Hydrolase (Cumd) Complexed With N-Butyrate

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.
PDB ID: 1UK7Download
MMDB ID: 29594
PDB Deposition Date: 2003/8/19
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1UK7: dimeric; determined by author
Molecular Components in 1UK7
Label Count Molecule
Proteins (2 molecules)
2-hydroxy-6-oxo-7-methylocta-2,4-dienoate Hydrolase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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