Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Purification and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing activity) from Alcaligenes faecalis N-38A

Article Abstract:

Research was conducted to examine the purification and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing activity) from Alcaligenes faecalis N-38A. The novelty of the 5-oxoprolinase was analyzed based on the decyclization reaction of L-pyroglutamate and the cyclization reaction of L-glutamate. Results provide strong evidence that the 5-oxoprolinase found in a cell extract of strain N-38A is a novel type of 5-oxoprolinase.

Author: Oyama, Hiroshi, Shin, Takashi, Murao, Sawao, Nishimura, Atsuhisa, Ozaki, Yasunori
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Enzymes, Adenosine triphosphate, ATP, Enzyme synthesis

User Contributions:

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

CAPTCHA


Novel bifunctional hyperthermostable carboxypeptidase/aminoacylase from Pyrococcus horikoshii OT3

Article Abstract:

An enzyme has been isolated from the thermophilic archaeon Pyrococcus horikoshii OT3 which is a new zinc-dependent metalloenzyme that has a structure similar to carboxypeptidase but a mechanism similar to aminoacylase. This indicates that carboxypeptidase and aminoacylase may have a common evolutionary origin.

Author: Ishikawa, Kazuhiko, Ishida, Hiroyasu, Matsui, Ikuo, Kawarabayashi, Yutaka, Kikuchi, Hisasi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001

User Contributions:

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

CAPTCHA


Molecular cloning, sequencing, and expression in Escherichia coli of the gene encoding a novel 5-oxoprolinase without ATP-hydrolyzing activity from Alcaligenes faecalis N-38A

Article Abstract:

A 5-oxoprolinase from Alcaligenes faecalis N38A with no sequence similarity to any other known protein is described. It is a zinc metalloenzyme with 402 amino acid residues and a mass of 46,163 Da.

Author: Nishimura, atsuhisa, Oyama, Hiroshi, Hamada, Takatoshi, Nobuoka, Katsunori, Shin, Takashi, Murao, Sawao, Oda, Kohei
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000

User Contributions:

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

CAPTCHA


Subjects list: Research, Microbial enzymes, Metalloenzymes
Similar abstracts:
  • Abstracts: Purification and characterization of an intracellular peroxidase from Streptomyces cyaneus. Purification and characterization of 2,6-beta-D-fructan 6-levanbiohydrolase from Streptomyces exfoliatus F3-2
  • Abstracts: Molecular cloning and characterization of a novel mosquitocidal protein gene from Bacillus thuringiensis subsp. fukuokaensis
  • Abstracts: Production, identification, and toxicity of gamma-decalactone and 4-hydroxydecanoic acid from Sporidiobolus spp
  • Abstracts: Detection and characterization of broad-host-range plasmids in environmental bacteria by PCR. Resuscitation by ferrioxamine E of stressed Salmonella enterica serovar Typhimurium from soil and water microcosms
  • Abstracts: Effects of surfactant mixtures, including Corexit 9527, on bacterial oxidation of acetate and alkanes in crude oil
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 © 2025 Advameg, Inc.