CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily

cDNA cloning, evolutionary relationships, and tissue distribution

Natalia Y. Kedishvili, Kirill M. Popov, Paul M. Rougraff, Yu Zhao, David Crabb, Robert Harris

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Three overlapping cDNA clones encoding methyl-malonate-semialdehyde dehydrogenase (MMSDH; 2-methyl-3-oxopropanoate:NAD+ oxidoreductase (CoApropanoylating); EC 1.2.1.27) have been isolated by screening a rat liver λgt 11 library with nondegenerate oligonucleotide probes synthesized according to polymerase chain rection-amplified portions coding for the N-terminal amino acid sequence of rat liver MMSDH. The three clones cover a total of 1942 base pairs of cDNA, with an open reading frame of 1569 base pairs. The authenticity of the composite cDNA was confirmed by a perfect match of 43 amino acids known from protein sequencing. The composite cDNA predicts a 503 amino acid mature protein with Mr = 55,330, consistent with previous estimates. Polymerase chain reaction was used to obtain the sequence of the 32 amino acids corresponding to the mitochondrial entry peptide. Northern blot analysis of total RNA from several rat tissues showed a single mRNA band of 3.8 kilobases. Relative mRNA levels were: kidney > liver > heart > muscle > brain, which differed somewhat from relative MMSDH protein levels determined by Western blot analysis: liver = kidney > heart > muscle > brain. A 1423-base pair cDNA clone encoding human MMSDH was isolated from a human liver λgt11 library. The human MMSDH cDNA contains an open reading frame of 1293 base pairs that encodes the protein from Leu-74 to the C terminus. Human and rat MMSDH share 89.6 and 97.7% identity in nucleotide and protein sequence, respectively. MMSDH clearly belongs to a superfamily of aldehyde dehydrogenases and is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenases.

Original languageEnglish
Pages (from-to)19724-19729
Number of pages6
JournalJournal of Biological Chemistry
Volume267
Issue number27
StatePublished - Sep 25 1992

Fingerprint

Methylmalonate-Semialdehyde Dehydrogenase (Acylating)
Aldehyde Dehydrogenase
Cloning
Tissue Distribution
Coenzyme A
Organism Cloning
Oxidoreductases
Complementary DNA
Tissue
Liver
Rats
Base Pairing
Amino Acids
Proteins
Clone Cells
Muscle
Betaine-Aldehyde Dehydrogenase
Brain
Open Reading Frames
Libraries

ASJC Scopus subject areas

  • Biochemistry

Cite this

CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily : cDNA cloning, evolutionary relationships, and tissue distribution. / Kedishvili, Natalia Y.; Popov, Kirill M.; Rougraff, Paul M.; Zhao, Yu; Crabb, David; Harris, Robert.

In: Journal of Biological Chemistry, Vol. 267, No. 27, 25.09.1992, p. 19724-19729.

Research output: Contribution to journalArticle

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abstract = "Three overlapping cDNA clones encoding methyl-malonate-semialdehyde dehydrogenase (MMSDH; 2-methyl-3-oxopropanoate:NAD+ oxidoreductase (CoApropanoylating); EC 1.2.1.27) have been isolated by screening a rat liver λgt 11 library with nondegenerate oligonucleotide probes synthesized according to polymerase chain rection-amplified portions coding for the N-terminal amino acid sequence of rat liver MMSDH. The three clones cover a total of 1942 base pairs of cDNA, with an open reading frame of 1569 base pairs. The authenticity of the composite cDNA was confirmed by a perfect match of 43 amino acids known from protein sequencing. The composite cDNA predicts a 503 amino acid mature protein with Mr = 55,330, consistent with previous estimates. Polymerase chain reaction was used to obtain the sequence of the 32 amino acids corresponding to the mitochondrial entry peptide. Northern blot analysis of total RNA from several rat tissues showed a single mRNA band of 3.8 kilobases. Relative mRNA levels were: kidney > liver > heart > muscle > brain, which differed somewhat from relative MMSDH protein levels determined by Western blot analysis: liver = kidney > heart > muscle > brain. A 1423-base pair cDNA clone encoding human MMSDH was isolated from a human liver λgt11 library. The human MMSDH cDNA contains an open reading frame of 1293 base pairs that encodes the protein from Leu-74 to the C terminus. Human and rat MMSDH share 89.6 and 97.7{\%} identity in nucleotide and protein sequence, respectively. MMSDH clearly belongs to a superfamily of aldehyde dehydrogenases and is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenases.",
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