The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine

ROSSOL I, Pühler A (1992)
J Bacteriol 174(9): 2968-2977.

Journal Article | Published | English

No fulltext has been uploaded

Author
;
Abstract
S-(beta-Aminoethyl)-cysteine (AEC) resistance was achieved in Corynebacterium glutamicum by cloning a chromosomal 1.5-kb EcoRV-BglII DNA fragment on a multicopy plasmid. DNA sequence analysis of the 1.5-kb DNA fragment revealed an open reading frame (ORF326) which represents the AEC resistance gene, designated aecD. The aecD gene directs the synthesis of a 36-kDa protein which was visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The aecD gene is a nonessential gene and mediates AEC resistance only in an amplified state. C. glutamicum strains harboring an amplified aecD gene can utilize AEC as an alternative nitrogen source, indicating that the AEC resistance mechanism is due to AEC degradation. Since the AEC degradation products analyzed by high-pressure liquid chromatography were found to be pyruvate and aminoethanethiol (cysteamine), it was concluded that the aecD gene encodes a C-S lyase with alpha,beta-elimination activity. Besides AEC, the C-S lyase was also able to use cysteine, cystine, and cystathionine as substrates.
Publishing Year
ISSN
PUB-ID

Cite this

ROSSOL I, Pühler A. The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine. J Bacteriol. 1992;174(9):2968-2977.
ROSSOL, I., & Pühler, A. (1992). The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine. J Bacteriol, 174(9), 2968-2977.
ROSSOL, I., and Pühler, A. (1992). The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine. J Bacteriol 174, 2968-2977.
ROSSOL, I., & Pühler, A., 1992. The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine. J Bacteriol, 174(9), p 2968-2977.
I. ROSSOL and A. Pühler, “The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine”, J Bacteriol, vol. 174, 1992, pp. 2968-2977.
ROSSOL, I., Pühler, A.: The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine. J Bacteriol. 174, 2968-2977 (1992).
ROSSOL, I, and Pühler, Alfred. “The Corynebacterium glutamicum aecD gene encodes a C-S lyase with alpha, beta-elimination activity that degrades aminoethylcysteine”. J Bacteriol 174.9 (1992): 2968-2977.
This data publication is cited in the following publications:
This publication cites the following data publications:

21 Citations in Europe PMC

Data provided by Europe PubMed Central.

Characteristics of methionine production by an engineered Corynebacterium glutamicum strain.
Park SD, Lee JY, Sim SY, Kim Y, Lee HS., Metab. Eng. 9(4), 2007
PMID: 17604670
Metabolic pathways and biotechnological production of L-cysteine.
Wada M, Takagi H., Appl. Microbiol. Biotechnol. 73(1), 2006
PMID: 17021879
The transcriptional regulator SsuR activates expression of the Corynebacterium glutamicum sulphonate utilization genes in the absence of sulphate.
Koch DJ, Ruckert C, Albersmeier A, Huser AT, Tauch A, Puhler A, Kalinowski J., Mol. Microbiol. 58(2), 2005
PMID: 16194234
Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum.
Marienhagen J, Kennerknecht N, Sahm H, Eggeling L., J. Bacteriol. 187(22), 2005
PMID: 16267288
Cometabolism of a nongrowth substrate: L-serine utilization by Corynebacterium glutamicum.
Netzer R, Peters-Wendisch P, Eggeling L, Sahm H., Appl. Environ. Microbiol. 70(12), 2004
PMID: 15574911
Genome-based analysis of biosynthetic aminotransferase genes of Corynebacterium glutamicum.
McHardy AC, Tauch A, Ruckert C, Puhler A, Kalinowski J., J. Biotechnol. 104(1-3), 2003
PMID: 12948641
The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.
Kalinowski J, Bathe B, Bartels D, Bischoff N, Bott M, Burkovski A, Dusch N, Eggeling L, Eikmanns BJ, Gaigalat L, Goesmann A, Hartmann M, Huthmacher K, Kramer R, Linke B, McHardy AC, Meyer F, Mockel B, Pfefferle W, Puhler A, Rey DA, Ruckert C, Rupp O, Sahm H, Wendisch VF, Wiegrabe I, Tauch A., J. Biotechnol. 104(1-3), 2003
PMID: 12948626
X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.
Clausen T, Schlegel A, Peist R, Schneider E, Steegborn C, Chang YS, Haase A, Bourenkov GP, Bartunik HD, Boos W., EMBO J. 19(5), 2000
PMID: 10698925
A physical and genetic map of the Corynebacterium glutamicum ATCC 13032 chromosome.
Bathe B, Kalinowski J, Puhler A., Mol. Gen. Genet. 252(3), 1996
PMID: 8842145
Recent advances in the physiology and genetics of amino acid-producing bacteria.
Jetten MS, Sinskey AJ., Crit. Rev. Biotechnol. 15(1), 1995
PMID: 7736600
MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase).
Zdych E, Peist R, Reidl J, Boos W., J. Bacteriol. 177(17), 1995
PMID: 7665481

2 References

Data provided by Europe PubMed Central.

DNA amplification and an unstable arginine gene in Streptomyces lividans 66.
Altenbuchner J, Cullum J., Mol. Gen. Genet. 195(1-2), 1984
PMID: 6092842

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 1569026
PubMed | Europe PMC

Search this title in

Google Scholar