1UKA
Crystal structure of a meta-cleavage product hydrolase (CumD) complexed with (S)-2-methylbutyrate
Summary for 1UKA
| Entry DOI | 10.2210/pdb1uka/pdb |
| Related | 1IUN 1IUO 1IUP 1UK6 1UK7 1UK8 1UK9 1UKB |
| Descriptor | 2-hydroxy-6-oxo-7-methylocta-2,4-dienoate hydrolase, 2-METHYLBUTANOIC ACID (3 entities in total) |
| Functional Keywords | aromatic compounds, cumene, isopropylbenzene, meta-cleavage compound hydrolase, polychlorinated biphenyl degradation, pseudomonas fluorescens ip01, alpha/beta-hydrolase, substrate specificity, cumene degradation, pcb, beta-ketolase, hydrolase |
| Biological source | Pseudomonas fluorescens |
| Total number of polymer chains | 1 |
| Total formula weight | 31608.74 |
| Authors | Fushinobu, S.,Jun, S.-Y.,Hidaka, M.,Nojiri, H.,Yamane, H.,Shoun, H.,Omori, T.,Wakagi, T. (deposition date: 2003-08-19, release date: 2004-09-14, Last modification date: 2023-10-25) |
| Primary citation | Fushinobu, S.,Jun, S.-Y.,Hidaka, M.,Nojiri, H.,Yamane, H.,Shoun, H.,Omori, T.,Wakagi, T. A Series of Crystal Structures of a meta-Cleavage Product Hydrolase from Pseudomonas fluorescens IP01 (CumD) Complexed with Various Cleavage Products BIOSCI.BIOTECHNOL.BIOCHEM., 69:491-498, 2005 Cited by PubMed 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. PubMed: 15784976DOI: 10.1271/bbb.69.491 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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