Previous Article | Next Article ![]()
Journal of Bacteriology, August 1999, p. 5119-5122, Vol. 181, No. 16
Department of Microbiology and Center for
Biological Resource Recovery, University of Georgia, Athens,
Georgia 30602-2605
Received 1 March 1999/Accepted 2 June 1999
A novel gene, designated ohb1, which encodes the
oxygen-sensitive and biotin-, ATP-, thiamin-, pyridoxal phosphate-, and
metal-ion-independent, reversible 4-hydroxybenzoate decarboxylase
(4-HOB-DC) from the obligate anaerobe Clostridium
hydroxybenzoicum JW/Z-1T was sequenced (GenBank
accession no. AF128880) and expressed. The 1,440-bp open reading frame
(ORF) (ohb1) encodes 480 amino acids. Major properties of
the heterologous enzyme (Ohb1) expressed in Escherichia
coli DH5
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Cloning, Characterization, and Expression of a
Novel Gene Encoding a Reversible 4-Hydroxybenzoate Decarboxylase
from Clostridium hydroxybenzoicum

and
were the same as those described for the native
4-HOB-DC (Z. He and J. Wiegel, J. Bacteriol. 178:3539-3543, 1996). The
deduced amino acid sequence shows up to 57% identity and up to 74%
similarity to hypothetical proteins deduced from ORFs in genomes from
bacteria and archaea, suggesting a possible novel gene family.
*
Corresponding author. Mailing address: University of
Georgia, Department of Microbiology, 215 Biological Science Building, Athens, GA 30602-2605. Phone: (706) 542-2651. Fax: (706) 542-2674. E-mail: JWIEGEL{at}arches.uga.edu.
Present address: Department of Biochemistry Center for Biomolecular
Structure Analysis, University of Texas Health Science Center at San
Antonio, San Antonio, TX 78284.
Present address: Air Force Research Lab, Tyndall Air Force Base,
FL 32403-5323.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»