Fushinobu_2005_Biosci.Biotechnol.Biochem_69_491

Reference

Title : A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products - Fushinobu_2005_Biosci.Biotechnol.Biochem_69_491
Author(s) : Fushinobu S , Jun SY , Hidaka M , Nojiri H , Yamane H , Shoun H , Omori T , Wakagi T
Ref : Biosci Biotechnol Biochem , 69 :491 , 2005
Abstract :

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.

PubMedSearch : Fushinobu_2005_Biosci.Biotechnol.Biochem_69_491
PubMedID: 15784976
Gene_locus related to this paper: psefl-cumD

Related information

Inhibitor Benzoic-acid
Substrate n-valerate    HODA-6-isopropyl    HODA-6-methyl    HODA-6-ethyl    HODA-6-phenyl
Gene_locus psefl-cumD
Family Carbon-carbon_bond_hydrolase
Structure 1UK6    1UK7    1UK8    1UK9    1UKA    1UKB
Chemical n-Butyrate    Isovalerate    2-methylbutanoic-acid

Citations formats

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

Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T (2005)
Biosci Biotechnol Biochem 69 :491