Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase

Article Abstract:

Researchers have created a mutant form of the enzyme tyrosine phenol-lyase from Erwinia herbicola that does not require L-tyrosine. This bacterium is used to produce L-DOPA for the treatment of Parkinson's disease, but the wild enzyme requires tyrosine. The tyrosine must then be separated from L-DOPA.

Author: Katayama, Takane, Suzuki, Hideyuki, Koyanagi, Takashi, Kumagai, Hidehiko
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Microbial genetic engineering, Industrial microbiology, Dopa, L-dopa

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Use of bacterial gamma-glutamyltranspeptidase for enzymatic synthesis of gamma-D-glutamyl compounds

Article Abstract:

An enzymatic method for synthesizing various gamma-D-glutamyl compounds efficiently and stereospecifically involving bacterial gamma-glutamyltranspeptidase with D-glutamine as a gamma-glutamyl donor was developed. By-products such as gamma-glutamylglutamine and gamma-glutamyl-gamma-glutamyltaurine were not synthesized and the yield of gamma-glutamyltaurine dramatically increased from 25 to 71%.

Author: Suzuki, Hideyuki, Kumagai, Hidehiko, Izuka, Shunsuke, Minami, Hiromichi, Miyakawa, Nobukazu, Ishihara, Sayaka
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Proteases, Bacteria, Glutamine

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


A single amino acid substitution converts gama-glutamyltranspeptidase to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase)

Article Abstract:

Escherichia coli, one of the residues that are conserved completely in glutamyltranspeptidase (GGT) but not in IV cephalosporin acylase and the GGT enzyme with the D433N mutation was sought and studied. It is concluded that the single amino acid substitution of GGT, Asp-433 to Asn, converted GGT to cephalosporin (GL-7-ACA) acylase.

Author: Suzuki, Hideyuki, Kumagai, Hidehiko, Ishihara, Sayaka, Miwa, Chinatsu
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
Pharmaceutical Preparation Manufacturing, Pharmaceutical preparations, Cephalosporin Preparations, Gene mutations, Gene mutation, Amino acids, Cephalosporins, Moxalactam, Cephaloridine

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research
Similar abstracts:
  • Abstracts: The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
  • Abstracts: PCR-based DNA amplification and presumptive detection of Escherichia coli O157:H7 with an internal fluorogenic probe and the 5' nuclease (TaqMan) assay
  • Abstracts: Regulation of invasive cell behavior by taiman, a Drosophila protein related to AlB1, a steroid receptor coactivator amplified in breast cancer
  • Abstracts: Strong, independent, quantitative genetic control of the timing of vegetative phase change and first flowering in Eucalyptus globulus ssp. globulus (Tasmanian Blue Gum)
  • Abstracts: Molecular characterization of Lactobacillus plantarum genes for beta-ketoacyl-acyl carrier protein synthase III (fabH) and acetyl coenzyme A carboxylase (accBCDA), which are essential for fatty acid biosynthesis
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2026 Advameg, Inc.