Cloning and functional analysis of adhS gene encoding quinoprotein alcohol dehydrogenase subunit III from Acetobacter pasteurianus SKU1108

2010 ◽  
Vol 138 (1-2) ◽  
pp. 39-49 ◽  
Author(s):  
Uraiwan Masud ◽  
Kazunobu Matsushita ◽  
Gunjana Theeragool
Keyword(s):  
Functional Analysis ◽  
Alcohol Dehydrogenase ◽  
Gene Encoding ◽  
Acetobacter Pasteurianus ◽  
Subunit Iii

scholarly journals Catalytic and Molecular Properties of the Quinohemoprotein Tetrahydrofurfuryl Alcohol Dehydrogenase from Ralstonia eutropha Strain Bo

2001 ◽  
Vol 183 (6) ◽  
pp. 1954-1960 ◽  
Author(s):  
Grit Zarnt ◽  
Thomas Schräder ◽  
Jan R. Andreesen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alcohol Dehydrogenase ◽  
Tertiary Structure ◽  
Ralstonia Eutropha ◽  
Signal Sequence ◽  
Substrate Inhibition ◽  
Catalytic Efficiency ◽  
Gene Encoding

ABSTRACT The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparentk cat/Km andK i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k cat/Km value of 788 × 104 M−1 s−1. The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases.

scholarly journals Molecular analysis of enterolysin a and entL gene cluster from natural isolate Enterococcus faecalis BGPT1-10P

Genetika ◽  
2013 ◽  
Vol 45 (2) ◽  
pp. 479-492 ◽  
Author(s):  
Katarina Veljovic ◽  
Amarela Terzic-Vidojevic ◽  
Maja Tolinacki ◽  
Milan Kojic ◽  
Ljubisa Topisirovic
Keyword(s):  
Functional Analysis ◽  
Nucleotide Sequence ◽  
Enterococcus Faecalis ◽  
Broad Spectrum ◽  
Candida Species ◽  
Genetic Information ◽  
Natural Isolate ◽  
Gene Encoding ◽  
Dna Fragment ◽  
Virulent Factor

Strain Enterococcus faecalis BGPT1-10P was isolated from artisanal semi-hard homemade cheese from Stara Planina, Serbia. Results showed that BGPT1-10P synthesized a heat labile bacteriocin with a broad spectrum of activity, including Listeria and Candida species. Further analysis revealed that synthesized bacteriocin is enterolysin A. Moreover, the entL gene encoding enterolysin A was found to be located on the chromosome. The entL gene was cloned and sequenced. Analysis of nucleotide sequence showed that the entL gene in natural isolate En. faecalis BGPT1-10P is identical to that of the entL gene described previously in En. faecalis LMG 2333. Within the cloned DNA fragment containing the entL gene, four ORFs were detected. One of them was identified as the scpE gene, which encodes a virulent factor staphopain peptidase. Functional analysis of the entL gene showed that the complete genetic information necessary for the synthesis of enterolysin A were directly linked solely to it. Strain BGPT1-10P also synthesized gelatinase and citolysin, and contained a set of virulent factors. In addition, BGPT1-10P carries the ermB and tetM genes conferring the resistance to erythromycin and tetracycline, respectively.

scholarly journals Functional analysis of the aroC gene encoding chorismate synthase from Xanthomonas oryzae pathovar oryzae

2012 ◽  
Vol 167 (6) ◽  
pp. 326-331 ◽  
Author(s):  
Eun-Sung Song ◽  
Young-Jin Park ◽  
Tae-Hwan Noh ◽  
Yeong-Tae Kim ◽  
Jeong-Gu Kim ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Xanthomonas Oryzae ◽  
Gene Encoding ◽  
Chorismate Synthase

scholarly journals Functional analysis of a gene encoding threonine synthase from rice

2010 ◽  
Vol 9 (8) ◽  
pp. 1122-1129 ◽  
Author(s):  
Shafiqul Islam Sikdar Md ◽  
Kim Jung Sup
Keyword(s):  
Functional Analysis ◽  
Gene Encoding ◽  
Threonine Synthase
Sign in / Sign up

Export Citation Format

Share Document