Abstract
The rat liver E1β subunit of the branched-chain α-ketoacid dehydrogenase complex has been cloned and sequenced. The amino acid sequence is highly conserved between rat, human and bovine forms of the protein. The β subunits of the branched-chain α-ketoacid dehydrogenase complex from rat and Pseudomonas putida, and the pyruvate dehydrogenase complex from human and Bacillus subtilis show sequence similarities which are shared with two other thiamine pyrophosphate-dependent enzymes, yeast (Hansenula polymorpha) formaldehyde transketolase and human transketolase. These similarities suggest that the β subunits may be involved in thiamine pyrophosphate binding.
| Original language | English |
|---|---|
| Pages (from-to) | 207-210 |
| Number of pages | 4 |
| Journal | Biochimica et Biophysica Acta - Gene Structure and Expression |
| Volume | 1132 |
| Issue number | 2 |
| DOIs | |
| State | Published - Sep 24 1992 |
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Keywords
- Branched chain α-ketoacid dehydrogenase
- cDNA
- Polymerase chain reaction
- Thiamine pyrophosphate
- α-Ketoacid dehydrogenase
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Genetics
- Structural Biology
Cite this
Molecular cloning of the E1β subunit of the rat branched chain α-ketoacid dehydrogenase. / Zhao, Y.; Kuntz, M. J.; Harris, Robert; Crabb, David.
In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1132, No. 2, 24.09.1992, p. 207-210.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular cloning of the E1β subunit of the rat branched chain α-ketoacid dehydrogenase
AU - Zhao, Y.
AU - Kuntz, M. J.
AU - Harris, Robert
AU - Crabb, David
PY - 1992/9/24
Y1 - 1992/9/24
N2 - The rat liver E1β subunit of the branched-chain α-ketoacid dehydrogenase complex has been cloned and sequenced. The amino acid sequence is highly conserved between rat, human and bovine forms of the protein. The β subunits of the branched-chain α-ketoacid dehydrogenase complex from rat and Pseudomonas putida, and the pyruvate dehydrogenase complex from human and Bacillus subtilis show sequence similarities which are shared with two other thiamine pyrophosphate-dependent enzymes, yeast (Hansenula polymorpha) formaldehyde transketolase and human transketolase. These similarities suggest that the β subunits may be involved in thiamine pyrophosphate binding.
AB - The rat liver E1β subunit of the branched-chain α-ketoacid dehydrogenase complex has been cloned and sequenced. The amino acid sequence is highly conserved between rat, human and bovine forms of the protein. The β subunits of the branched-chain α-ketoacid dehydrogenase complex from rat and Pseudomonas putida, and the pyruvate dehydrogenase complex from human and Bacillus subtilis show sequence similarities which are shared with two other thiamine pyrophosphate-dependent enzymes, yeast (Hansenula polymorpha) formaldehyde transketolase and human transketolase. These similarities suggest that the β subunits may be involved in thiamine pyrophosphate binding.
KW - Branched chain α-ketoacid dehydrogenase
KW - cDNA
KW - Polymerase chain reaction
KW - Thiamine pyrophosphate
KW - α-Ketoacid dehydrogenase
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UR - http://www.scopus.com/inward/citedby.url?scp=0026784041&partnerID=8YFLogxK
U2 - 10.1016/0167-4781(92)90014-Q
DO - 10.1016/0167-4781(92)90014-Q
M3 - Article
C2 - 1390893
AN - SCOPUS:0026784041
VL - 1132
SP - 207
EP - 210
JO - Biochimica et Biophysica Acta - Gene Structure and Expression
JF - Biochimica et Biophysica Acta - Gene Structure and Expression
SN - 0167-4781
IS - 2
ER -