Physical and biochemical characterization of the cloned LYS5 gene required for ?-aminoadipate reductase activity in the lysine biosynthetic pathway of Saccharomyces cerevisiae

1992 ◽  
Vol 21 (1) ◽  
pp. 13-16 ◽  
Author(s):  
Sudha Rajnarayan ◽  
Jack C. Vaughn ◽  
J. K. Bhattacharjee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biosynthetic Pathway ◽  
Biochemical Characterization ◽  
Reductase Activity ◽  
Lys5 Gene

scholarly journals Characterization of an Escherichia coli K12 mutant that is sensitive to chlorate when grown aerobically

1978 ◽  
Vol 176 (2) ◽  
pp. 553-561 ◽  
Author(s):  
G Giordano ◽  
L Grillet ◽  
R Rosset ◽  
J H Dou ◽  
E Azoulay ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway ◽  
Formate Dehydrogenase ◽  
Biochemical Characterization ◽  
Reductase Activity ◽  
Growth Conditions ◽  
Aerobic Growth ◽  
Benzyl Viologen ◽  
Genetic Lesion

Escherichia coli can normally grow aerobically in the presence of chlorate; however, mutants can be isolated that can no longer grow under these conditions. We present here the biochemical characterization of one such mutant and show that the primary genetic lesion occurs in the ubiquinone-8-biosynthetic pathway. As a consequence of this, under aerobic growth conditions the mutant is apparently unable to synthesize formate dehydrogenase, but can synthesize a Benzyl Viologen-dependent nitrate reductase activity. The nature of this activity is discussed.

Cloning and biochemical characterization of LYS5 gene of Saccharomyces cerevisiae

1988 ◽  
Vol 13 (4) ◽  
pp. 299-304 ◽  
Author(s):  
Christopher W. Borell ◽  
J. K. Bhattacharjee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biochemical Characterization ◽  
Lys5 Gene

scholarly journals Structural and Biochemical Characterization of the Salicylyl-acyltranferase SsfX3 from a Tetracycline Biosynthetic Pathway

2011 ◽  
Vol 286 (48) ◽  
pp. 41539-41551 ◽  
Author(s):  
Lauren B. Pickens ◽  
Michael R. Sawaya ◽  
Huma Rasool ◽  
Inna Pashkov ◽  
Todd O. Yeates ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Biochemical Characterization

Genetic and biochemical characterization of Saccharomyces cerevisiae mutants resistant to trifluoroleucine

1997 ◽  
Vol 148 (7) ◽  
pp. 613-623 ◽  
Author(s):  
E. Casalone ◽  
G. Fia ◽  
C. Barberio ◽  
D. Cavalieri ◽  
L. Turbanti ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Biochemical Characterization

scholarly journals Biochemical Characterization of the CDP-D-Arabinitol Biosynthetic Pathway in Streptococcus pneumoniae 17F

2012 ◽  
Vol 194 (8) ◽  
pp. 1868-1874 ◽  
Author(s):  
Q. Wang ◽  
Y. Xu ◽  
A. V. Perepelov ◽  
Y. A. Knirel ◽  
P. R. Reeves ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Biosynthetic Pathway ◽  
Biochemical Characterization

scholarly journals Molecular Characterization of Saccharomyces cerevisiae TFIID

2002 ◽  
Vol 22 (16) ◽  
pp. 6000-6013 ◽  
Author(s):  
Steven L. Sanders ◽  
Krassimira A. Garbett ◽  
P. Anthony Weil
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Molecular Mass ◽  
Molecular Characterization ◽  
Biochemical Characterization ◽  
Gel Filtration ◽  
Calculated Molecular Mass ◽  
General Transcription Factor

ABSTRACT We previously defined Saccharomyces cerevisiae TFIID as a 15-subunit complex comprised of the TATA binding protein (TBP) and 14 distinct TBP-associated factors (TAFs). In this report we give a detailed biochemical characterization of this general transcription factor. We have shown that yeast TFIID efficiently mediates both basal and activator-dependent transcription in vitro and displays TATA box binding activity that is functionally distinct from that of TBP. Analyses of the stoichiometry of TFIID subunits indicated that several TAFs are present at more than 1 copy per TFIID complex. This conclusion was further supported by coimmunoprecipitation experiments with a systematic family of (pseudo)diploid yeast strains that expressed epitope-tagged and untagged alleles of the genes encoding TFIID subunits. Based on these data, we calculated a native molecular mass for monomeric TFIID. Purified TFIID behaved in a fashion consistent with this calculated molecular mass in both gel filtration and rate-zonal sedimentation experiments. Quite surprisingly, although the TAF subunits of TFIID cofractionated as a single complex, TBP did not comigrate with the TAFs during either gel filtration chromatography or rate-zonal sedimentation, suggesting that TBP has the ability to dynamically associate with the TFIID TAFs. The results of direct biochemical exchange experiments confirmed this hypothesis. Together, our results represent a concise molecular characterization of the general transcription factor TFIID from S. cerevisiae.

Structural and biochemical characterization of two novel enzymes with promiscuous ene-reductase activity

2014 ◽  
Vol 31 ◽  
pp. S20
Author(s):  
Tea Pavkov-Keller ◽  
Alexandra Binter ◽  
Steinkellner Georg ◽  
Christian C. Gruber ◽  
Kerstin Steiner ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Reductase Activity

Discovery and Biocatalytic Application of a PLP-Dependent Amino Acid γ-Substitution Enzyme that Catalyzes C-C Bond Formation

2020 ◽  
Author(s):  
Mengbin Chen ◽  
Chun-Ting Liu ◽  
Yi Tang
Keyword(s):  
Amino Acids ◽  
Biosynthetic Pathway ◽  
Pyridoxal Phosphate ◽  
Biochemical Characterization ◽  
Indole Alkaloid ◽  
Building Blocks ◽  
Nucleophilic Attack ◽  
Keto Esters ◽  
Key Enzyme

Pyridoxal phosphate (PLP)-dependent enzymes can catalyze various transformations of amino acids at alpha, beta, and gamma positions. These versatile enzymes are prominently involved in the biosynthesis of nonproteinogenic amino acids as building blocks of natural products, and are attractive biocatalysts. Here, we report the discovery of a two-step enzymatic synthesis of (2<i>S, </i>6<i>S</i>)-6-methyl pipecolate <b>1</b>, from the biosynthetic pathway of indole alkaloid citrinadin. The key enzyme CndF is PLP-dependent and catalyzes synthesis of (<i>S</i>)-2-amino-6-oxoheptanoate <b>3</b> that is in equilibrium with the cyclic Schiff base. The second enzyme CndE is a stereoselective imine reductase that gives <b>1</b>. Biochemical characterization of CndF showed this enzyme performs gamma-elimination of <i>O</i>-acetyl L-homoserine to generate the vinylglycine ketimine, which is subjected to nucleophilic attack by acetoacetate to form the new C<sub>gamma</sub>-C<sub>delta</sub> bond in <b>3 </b>and complete the gamma-substitution reaction. CndF displays substrate promiscuity towards different beta-keto carboxylate and esters. Using a recombinant <i>Aspergillus </i>strain expressing CndF and CndE, feeding various alkyl-beta-keto esters led to the biosynthesis of 6-substituted L-pipecolates. The discovery of CndF expands the repertoire of reactions that can be catalyzed by PLP-dependent enzymes.

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