Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme.
Abstract: The primary structure of the mitochondrial form of horse liver aldehyde dehydrogenase has been determined, utilizing peptide analyses and homology with other enzyme forms. The subunit exhibits N-terminal heterogeneity in size similar to that for the corresponding human mitochondrial protein, the longest form having 500 residues. Catalase was identified as a contaminant of the preparations. All four pairs within a set of aldehyde dehydrogenases can now be compared, including the same two species variants (horse and human) for both the cytosolic and mitochondrial enzyme, revealing characteristic differences although Cys-302 and other segments of presumed functional importance are unchanged. The cytosolic and mitochondrial enzymes are clearly different (172 exchanges in the horse pair; 160 exchanges in the human pair) and the mitochondrial forms are more conserved (28 exchanges of 500 residues) than the cytosolic ones (43 exchanges). Distributions of the residue substitutions also differ between the two enzyme types. These results suggest a comparatively distant separation of the cytosolic and mitochondrial enzymes into forms with separate functional constraints that are more strict on the mitochondrial than the cytosolic enzyme. Unexpectedly, positions with residues unique to one of the four enzymes are about twice as common in both of the horse proteins than in either of the human proteins. This difference may reflect a general pattern for human/non-human proteins, showing that not only functional properties of the protein, but also other factors, such as generation time (longer in man than in horse), are important for enzyme divergence.
Publication Date: 1988-03-15 PubMed ID: 3350012DOI: 10.1111/j.1432-1033.1988.tb13920.xGoogle Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study examines the structure of mitochondrial aldehyde dehydrogenase from a horse liver, comparing it with human variants of this enzyme. It suggests differences in the functionality and constraints between the cytosolic and mitochondrial enzymes and explores the impact of generation time on enzyme divergence.
Methodology and Findings
- The researchers determined the primary structure of the mitochondrial form of horse liver aldehyde dehydrogenase through peptide analyses and homology with other enzyme forms.
- The enzyme demonstrated N-terminal heterogeneity in size, similar to the human mitochondrial version, with the longest form comprising 500 residues.
- Catalase was detected as a contaminant in the preparations.
- The study also compared all four pairs of aldehyde dehydrogenases, including two species variants (horse and human) for both the cytosolic and mitochondrial enzymes.
- Interestingly, certain segments of presumed functional importance, such as Cys-302, remained unchanged, yet there were notable differences between the enzymes.
Comparisons Between the Enzymes
- The cytosolic and mitochondrial enzymes were different, with 172 exchanges in horse pairs and 160 exchanges in human pairs.
- The mitochondrial forms were more conserved, with only 28 exchanges of 500 residues, compared to the cytosolic ones, which had 43 exchanges.
- The distribution of residue substitutions also varied between the two enzyme types.
Suggestions from the Study
- The findings suggest a considerable separation between the cytosolic and mitochondrial enzymes. The functional constraints seem stricter on the mitochondrial enzyme.
- Unexpectedly, positions with residues unique to one of the four enzymes were about twice as common in horse proteins as in human proteins.
- This difference potentially indicates general trends in human/non-human proteins, demonstrating that factors beyond the protein’s functional properties, such as generation time, are significant for enzyme divergence. The generation time is longer in humans than in horses, which may affect enzyme evolution.
Cite This Article
APA
Johansson J, von Bahr-Lindström H, Jeck R, Woenckhaus C, Jörnvall H.
(1988).
Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme.
Eur J Biochem, 172(3), 527-533.
https://doi.org/10.1111/j.1432-1033.1988.tb13920.x Publication
Researcher Affiliations
- Department of Chemistry I, Karolinska Institutet, Stockholm.
MeSH Terms
- Aldehyde Dehydrogenase / analysis
- Amino Acid Sequence
- Animals
- Base Composition
- Cytosol / enzymology
- Horses
- Humans
- Mitochondria, Liver / enzymology
- Molecular Sequence Data
- Peptide Fragments / analysis
- Peptides / analysis
- Species Specificity
Citations
This article has been cited 14 times.- Shiue Y-L, Millon LV, Skow LC, Honeycutt D, Murray JD, Bowling AT. Synteny and regional marker order assignment of 26 type I and microsatellite markers to the horse X- and Y-chromosomes.. Chromosome Res 2000;8(1):45-55.
- Ni L, Zhou J, Hurley TD, Weiner H. Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms.. Protein Sci 1999 Dec;8(12):2784-90.
- Hempel J, Nicholas H, Lindahl R. Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework.. Protein Sci 1993 Nov;2(11):1890-900.
- Denome SA, Stanley DC, Olson ES, Young KD. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway.. J Bacteriol 1993 Nov;175(21):6890-901.
- Chen JH, Kabbouh M, Fisher MJ, Rees HH. Induction of an inactivation pathway for ecdysteroids in larvae of the cotton leafworm, Spodoptera littoralis.. Biochem J 1994 Jul 1;301 ( Pt 1)(Pt 1):89-95.
- Powlowski J, Shingler V. Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600.. Biodegradation 1994 Dec;5(3-4):219-36.
- Loomes KM, Kitson TM. Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiol-modifying reagents.. Biochem J 1989 Jul 1;261(1):281-4.
- Poole RC, Halestrap AP. Purification of aldehyde dehydrogenase from rat liver mitochondria by alpha-cyanocinnamate affinity chromatography.. Biochem J 1989 Apr 1;259(1):105-10.
- Weretilnyk EA, Hanson AD. Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought.. Proc Natl Acad Sci U S A 1990 Apr;87(7):2745-9.
- Blatter EE, Tasayco ML, Prestwich G, Pietruszko R. Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone.. Biochem J 1990 Dec 1;272(2):351-8.
- Saigal D, Cunningham SJ, Farrés J, Weiner H. Molecular cloning of the mitochondrial aldehyde dehydrogenase gene of Saccharomyces cerevisiae by genetic complementation.. J Bacteriol 1991 May;173(10):3199-208.
- Kitson TM, Hill JP, Midwinter GG. Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase.. Biochem J 1991 Apr 1;275 ( Pt 1)(Pt 1):207-10.
- Abriola DP, MacKerell AD Jr, Pietruszko R. Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase.. Biochem J 1990 Feb 15;266(1):179-87.
- Priefert H, Krüger N, Jendrossek D, Schmidt B, Steinbüchel A. Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus.. J Bacteriol 1992 Feb;174(3):899-907.
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