|1.||Tang, Gong-Li: 2 articles (10/2014 - 03/2014)|
|2.||He, Hai-Yan: 2 articles (10/2014 - 03/2014)|
|3.||Tang, Man-Cheng: 2 articles (10/2014 - 03/2014)|
|4.||Yuan, Hua: 1 article (10/2014)|
|5.||Zhang, Xiao-Sheng: 1 article (08/2014)|
|6.||Liu, Shui-Ping: 1 article (08/2014)|
|7.||Ran, Xin-Xin: 1 article (08/2014)|
|8.||Chen, Wei-Bin: 1 article (08/2014)|
|9.||Jiang, Xin-Hang: 1 article (08/2014)|
|10.||Wang, Yue-Yue: 1 article (08/2014)|
|1.||Dehydration (Water Stress)
08/25/2014 - "The known functions of type II thioesterases (TEIIs) in type I polyketide synthases (PKSs) include selecting of starter acyl units, removal of aberrant extender acyl units, releasing of final products, and dehydration of polyketide intermediates. "
12/10/2013 - "On the other hand, when EryACP6, from the sixth module of the erythromycin polyketide synthase, is substituted for RifACP10, RifDH10 stereospecifically dehydrates only (2R,3R)-2-methyl-3-hydroxypentanoyl-EryACP6 to give exclusively (E)-2-methyl-2-pentenoyl-EryACP6, with no detectable dehydration of any of the other three diastereomeric, EryACP6-bound, diketides. "
12/10/2013 - "RifDH10, the dehydratase domain from the terminal module of the rifamycin polyketide synthase, catalyzes the stereospecific syn dehydration of the model substrate (2S,3S)-2-methyl-3-hydroxypentanoyl-RifACP10, resulting in the exclusive formation of (E)-2-methyl-2-pentenoyl-RifACP10. "
10/13/2014 - "Polyketide synthases (PKSs) usually employ a ketoreductase (KR) to catalyze the reduction of a β-keto group, followed by a dehydratase (DH) that drives the dehydration to form a double bond between the α- and β-carbon atoms. "
03/26/2014 - "Modular polyketide synthases (PKSs) are well known to use ketosynthase (KS)-driven carbon-carbon bond formation, dehydratase-mediated dehydration to form double bonds, and product release by thioesterase (TE), all of which are regarded as the "canonical" roles for most polyketide biosyntheses. "
|2.||Contagious Ecthyma (Orf)
08/16/1993 - "A Bacillus subtilis large ORF coding for a polypeptide highly similar to polyketide synthases."
02/15/1992 - "The predicted gene product of ORF B is a polypeptide of 374417 Da (3568 amino acids), which is highly similar to the product of ORF A and which likewise contains a number of separate domains, each with substantial amino acid sequence similarity to components of known fatty-acid synthases and polyketide synthases. "
02/15/1992 - "Sequencing of the eryA region of the erythromycin biosynthetic gene cluster from Saccharopolyspora erythraea has revealed another structural gene (ORF B), in addition to the previously characterised ORF A, which appears to encode a component of 6-deoxyerythronolide-B synthase, the enzyme that catalyses the first stage in the biosynthesis of the polyketide antibiotic erythromycin A. "
01/01/2011 - "tuberculosis and identified 11 putative in-vivo induced genes encoding for immunogenic proteins of diverse functions; these included transcriptional regulators (Rv1460 and Rv2565), biosynthesis and macromolecule metabolism (leuD, guaB1, plcC, hupB and glyS), polyketide synthases (pks6 and pks9), cell processes (ctpA) and one with unknown function (Rv3701c). "
|2.||Proteins (Proteins, Gene)
|5.||4- ((1,4,8,11- tetraazacyclotetradec- 1- yl)methyl)benzoic acid