Nucleotide sequence of the respiratory d-lactate dehydrogenase gene of Escherichia coli

Content Provider	Scilit
Author	Campbell, Hugh D. Rogers, Bruce L. Young, Ian G.
Copyright Year	1984
Description	Journal: Journal of Biological Inorganic Chemistry The structural gene for the respiratory d-lactate dehydrogenase of Escherichia coli, a membrane-bound flavoenzyme, has been subcloned from a 7 × $10^{3}$-base-pair chromosomal HindIII fragment containing the gene [Young, I. G., Jaworowski, A., and Poulis, M. (1982) Biochemistry 21, 2092–2095]. The complete nucleotide sequence of the 2340-base-pair PstI-SmaI subclone has been determined on both strands by the dideoxy chain termination method. A single large open reading frame is present in the nucleotide sequence. The reading frame is preceded by a good ribosome binding site and numerous possible promoter sequences, and is followed by a typical rho-independent termination sequence. The reading frame predicts that the d-lactate dehydrogenase polypeptide consists of 571 amino acids (including the initiating methionine residue) with $M_{r}$= 64613. The protein does not have a low overall polarity, nor does it contain unusually hydrophobic stretches. It appears to contain a short repeat which is homologous with the well characterized l-lactate dehydrogenases in the vicinity of the 'essential' cysteine residue. Apart from this, homology with other proteins of known sequence has not been detected.
Related Links	https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1984.tb08473.x
Ending Page	373
Page Count	7
Starting Page	367
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1984.tb08473.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	144
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1984-10-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biotechnology and Microbiology Lactate Dehydrogenase
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry