Literature DB >> 6745443

Human liver mitochondrial aldehyde dehydrogenase: a C-terminal segment positions and defines the structure corresponding to the one reported to differ in the Oriental enzyme variant.

J Hempel, R Kaiser, H Jörnvall.   

Abstract

A C-terminal segment of mitochondrial human liver aldehyde dehydrogenase was characterized. The results prove that a central part of this segment largely but not completely agrees with a structure of a tryptic peptide previously reported for the same isoenzyme. This part corresponds to a segment that contains the exchanged residue in the functionally deficient Oriental variant of mitochondrial aldehyde dehydrogenase [(1984) Proc. Natl. Acad. Sci. USA 81, 258-261]. The data suggest important functions for the C-terminal region of aldehyde dehydrogenase, clarify previously inconsistent results, and establish this structure in the typical enzyme, including the position corresponding to the mutation in the functional variant.

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Year:  1984        PMID: 6745443     DOI: 10.1016/0014-5793(84)80807-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  9 in total

1.  Genetic polymorphism and activities of human lung alcohol and aldehyde dehydrogenases: implications for ethanol metabolism and cytotoxicity.

Authors:  S J Yin; C S Liao; C M Chen; F T Fan; S C Lee
Journal:  Biochem Genet       Date:  1992-04       Impact factor: 1.890

2.  The aldehyde dehydrogenase ALDH2*2 allele exhibits dominance over ALDH2*1 in transduced HeLa cells.

Authors:  Q Xiao; H Weiner; T Johnston; D W Crabb
Journal:  J Clin Invest       Date:  1995-11       Impact factor: 14.808

3.  The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases turnover of the enzyme tetramers in a dominant fashion.

Authors:  Q Xiao; H Weiner; D W Crabb
Journal:  J Clin Invest       Date:  1996-11-01       Impact factor: 14.808

4.  Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases.

Authors:  José Salud Rodríguez-Zavala; Abdellah Allali-Hassani; Henry Weiner
Journal:  Protein Sci       Date:  2006-06       Impact factor: 6.725

5.  CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity.

Authors:  Laura Strittmatter; Yang Li; Nathan J Nakatsuka; Sarah E Calvo; Zenon Grabarek; Vamsi K Mootha
Journal:  Hum Mol Genet       Date:  2013-12-11       Impact factor: 6.150

6.  Enzymatic activity of atypical Oriental types of aldehyde dehydrogenases.

Authors:  A Yoshida; V Davé
Journal:  Biochem Genet       Date:  1985-08       Impact factor: 1.890

7.  aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp.

Authors:  J Xu; R C Johnson
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

8.  The association of alcohol and alcohol metabolizing gene variants with diabetes and coronary heart disease risk factors in a white population.

Authors:  Lise Lotte N Husemoen; Torben Jørgensen; Knut Borch-Johnsen; Torben Hansen; Oluf Pedersen; Allan Linneberg
Journal:  PLoS One       Date:  2010-08-05       Impact factor: 3.240

9.  Modification of the Associations of Alcohol Intake With Serum Low-Density Lipoprotein Cholesterol and Triglycerides by ALDH2 and ADH1B Polymorphisms in Japanese Men.

Authors:  Tae Sasakabe; Kenji Wakai; Sayo Kawai; Asahi Hishida; Mariko Naito; Sadao Suzuki; Yora Nindita; Kokichi Arisawa; Yoshikuni Kita; Megumi Hara; Nagato Kuriyama; Akie Hirata; Haruo Mikami; Isao Oze; Michiaki Kubo; Hideo Tanaka; Nobuyuki Hamajima
Journal:  J Epidemiol       Date:  2017-11-25       Impact factor: 3.211

  9 in total

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