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Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis.
FEBS Lett. 2012 Feb 17; 586(4):337-43.FL

Abstract

Cinnamyl alcohol dehydrogenase is a zinc- and NADPH-dependent dehydrogenase catalyzing the reversible conversion of p-hydroxycinnamaldehydes to their corresponding hydroxycinnamyl alcohols. A CAD homolog from Helicobacter pylori (HpCAD) possesses broad substrate specificities like the plant CADs and additionally a dismutation activity converting benzaldehyde to benzyl alcohol and benzoic acid. We have determined the crystal structure of HpCAD complexed with NADP(H) at 2.18Å resolution to get a better understanding of this class of CAD outside of plants. The structure of HpCAD is highly homologous to the sinapyl alcohol dehydrogenase and the plant CAD with well-conserved residues involved in catalysis and zinc binding. However, the NADP(H) binding mode of the HpCAD has been found to be significantly different from those of plant CADs.

Authors+Show Affiliations

Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22269576

Citation

Seo, Kyung Hye, et al. "Unusual NADPH Conformation in the Crystal Structure of a Cinnamyl Alcohol Dehydrogenase From Helicobacter Pylori in Complex With NADP(H) and Substrate Docking Analysis." FEBS Letters, vol. 586, no. 4, 2012, pp. 337-43.
Seo KH, Zhuang N, Chen C, et al. Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis. FEBS Lett. 2012;586(4):337-43.
Seo, K. H., Zhuang, N., Chen, C., Song, J. Y., Kang, H. L., Rhee, K. H., & Lee, K. H. (2012). Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis. FEBS Letters, 586(4), 337-43. https://doi.org/10.1016/j.febslet.2012.01.020
Seo KH, et al. Unusual NADPH Conformation in the Crystal Structure of a Cinnamyl Alcohol Dehydrogenase From Helicobacter Pylori in Complex With NADP(H) and Substrate Docking Analysis. FEBS Lett. 2012 Feb 17;586(4):337-43. PubMed PMID: 22269576.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis. AU - Seo,Kyung Hye, AU - Zhuang,Ningning, AU - Chen,Cong, AU - Song,Jae-Young, AU - Kang,Hyung-Lyun, AU - Rhee,Kwang-Ho, AU - Lee,Kon Ho, Y1 - 2012/01/21/ PY - 2011/10/26/received PY - 2011/12/31/revised PY - 2012/01/12/accepted PY - 2012/1/25/entrez PY - 2012/1/25/pubmed PY - 2012/4/10/medline SP - 337 EP - 43 JF - FEBS letters JO - FEBS Lett. VL - 586 IS - 4 N2 - Cinnamyl alcohol dehydrogenase is a zinc- and NADPH-dependent dehydrogenase catalyzing the reversible conversion of p-hydroxycinnamaldehydes to their corresponding hydroxycinnamyl alcohols. A CAD homolog from Helicobacter pylori (HpCAD) possesses broad substrate specificities like the plant CADs and additionally a dismutation activity converting benzaldehyde to benzyl alcohol and benzoic acid. We have determined the crystal structure of HpCAD complexed with NADP(H) at 2.18Å resolution to get a better understanding of this class of CAD outside of plants. The structure of HpCAD is highly homologous to the sinapyl alcohol dehydrogenase and the plant CAD with well-conserved residues involved in catalysis and zinc binding. However, the NADP(H) binding mode of the HpCAD has been found to be significantly different from those of plant CADs. SN - 1873-3468 UR - https://www.unboundmedicine.com/medline/citation/22269576/Unusual_NADPH_conformation_in_the_crystal_structure_of_a_cinnamyl_alcohol_dehydrogenase_from_Helicobacter_pylori_in_complex_with_NADP_H__and_substrate_docking_analysis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(12)00053-1 DB - PRIME DP - Unbound Medicine ER -