Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444906039199
Title: The 1.8 Å resolution structure of hydroxycinnamoyl-coenzyme a hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin
Authors: Leonard, P.M
Brzozowski, A.M
Lebedev, A
Marshall, C.M
Smith, D.J
Verma, C.S 
Walton, N.J
Grogan, G
Keywords: Pseudomonas fluorescens
4 hydroxycinnamoyl CoA hydratase lyase
4-hydroxycinnamoyl-CoA hydratase-lyase
acyl coenzyme A
benzaldehyde derivative
cinnamoyl coenzyme A
cinnamoyl-coenzyme A
enoyl coenzyme A hydratase
feruloyl CoA
feruloyl-CoA
hydrolyase
vanillin
article
binding site
catalysis
chemical structure
chemistry
enzymology
metabolism
protein folding
protein quaternary structure
protein secondary structure
Pseudomonas fluorescens
X ray crystallography
Acyl Coenzyme A
Benzaldehydes
Binding Sites
Catalysis
Crystallography, X-Ray
Enoyl-CoA Hydratase
Hydro-Lyases
Models, Molecular
Protein Folding
Protein Structure, Quaternary
Protein Structure, Secondary
Pseudomonas fluorescens
Issue Date: 2006
Citation: Leonard, P.M, Brzozowski, A.M, Lebedev, A, Marshall, C.M, Smith, D.J, Verma, C.S, Walton, N.J, Grogan, G (2006). The 1.8 Å resolution structure of hydroxycinnamoyl-coenzyme a hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin. Acta Crystallographica Section D: Biological Crystallography 62 (12) : 1494-1501. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444906039199
Rights: Attribution 4.0 International
Abstract: The crystal structure of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) from Pseudomonas fluorescens AN103 has been solved to 1.8 Å resolution. HCHL is a member of the crotonase superfamily and catalyses the hydration of the acyl-CoA thioester of ferulic acid [3-(4-hydroxy-3-methoxy-phenyl)prop-2-enoic acid] and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde). The structure contains 12 molecules in the asymmetric unit, in which HCHL assumes a hexameric structure of two stacked trimers. The substrate, feruloyl-CoA, was modelled into the active site based on the structure of enoyl-CoA hydratase bound to the feruloyl-CoA-like substrate 4-(N,N-dimethylamino)-cinnamoyl-CoA (PDB code). Feruloyl-CoA was bound in this model between helix 3 of the A subunit and helix 9 of the B subunit. A highly ordered structural water in the HCHL structure coincided with the thioester carbonyl of feruloyl-CoA in the model, suggesting that the oxyanion hole for stabilization of a thioester-derived enolate, characteristic of coenzyme-A dependent members of the crotonase superfamily, is conserved. The model also suggested that a strong hydrogen bond between the phenolic hydroxyl groups of feruloyl-CoA and BTyr239 may be an important determinant of the enzyme's ability to discriminate between the natural substrate and cinnamoyl-CoA, which is not a substrate. © International Union of Crystallography, 2006.
Source Title: Acta Crystallographica Section D: Biological Crystallography
URI: https://scholarbank.nus.edu.sg/handle/10635/181053
ISSN: 0907-4449
DOI: 10.1107/S0907444906039199
Rights: Attribution 4.0 International
Appears in Collections:Staff Publications
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