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

• Main Authors: Leonard, P.M, Brzozowski, A.M, Lebedev, A, Marshall, C.M, Smith, D.J, Verma, C.S, Walton, N.J, Grogan, G
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: 2020
• Subjects: 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; 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
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/181053
• Institution: National University of Singapore

10.1107/S0907444906039199