scholarly journals 4,4′-Diapophytoene Desaturase: Catalytic Properties of an Enzyme from the C30 Carotenoid Pathway ofStaphylococcus aureus

1999 ◽  
Vol 181 (19) ◽  
pp. 6184-6187 ◽  
Author(s):  
Axel Raisig ◽  
Gerhard Sandmann

ABSTRACT Staphylococcus aureus synthesizes C30carotenoids. Their formation involves the introduction of three double bonds, which is catalyzed by a single enzyme. This enzyme, 4,4′-diapophytoene desaturase from S. aureus, was overexpressed in Escherichia coli and purified in one step by affinity chromatography, and then the protein was characterized with respect to substrate specificity, cofactor requirement, and oligomerization.

1981 ◽  
Vol 256 (11) ◽  
pp. 5633-5637 ◽  
Author(s):  
H. Cudny ◽  
R. Zaniewski ◽  
M.P. Deutscher

2012 ◽  
Vol 534 ◽  
pp. 78-81
Author(s):  
Ting Wei Hu ◽  
Shao Yun Shan ◽  
Shi Mei Yang ◽  
Li Hong Jiang ◽  
Ya Ming Wang ◽  
...  

Polyaniline(PANI)/TiO2 nanocomposites are successful synthesized by one step-interfacial polymerization method. Morphologies and structures of the nanocomposites are characterized using SEM, FTIR, and XRD. The antibacterial properties of PANI/TiO2 nanocomposites on Staphylococcus aureus, Bacillus subtilis, Escherichia coli, Bacillus megateriu and Bacillus cereus are tested. The effect of molar ratio of aniline and tetrabutyl titanate on structures and antibacterial properties are also been explored. The results show that the content of tetrabutyl titanate has a obvious influence on structure and morphologies of the nanocomposites. PANI/TiO2 nanocomposites have antibacterial properties especially on Staphylococcus aureus and Escherichia coli, which shows a best antibacterial property when the molar ratio of aniline to tetrabutyl titanate is 3:2.


2002 ◽  
Vol 184 (23) ◽  
pp. 6690-6699 ◽  
Author(s):  
Daisuke Umeno ◽  
Alexander V. Tobias ◽  
Frances H. Arnold

ABSTRACT The C30 carotene synthase CrtM from Staphylococcus aureus and the C40 carotene synthase CrtB from Erwinia uredovora were swapped into their respective foreign C40 and C30 biosynthetic pathways (heterologously expressed in Escherichia coli) and evaluated for function. Each displayed negligible ability to synthesize the natural carotenoid product of the other. After one round of mutagenesis and screening, we isolated 116 variants of CrtM able to synthesize C40 carotenoids. In contrast, we failed to find a single variant of CrtB with detectable C30 activity. Subsequent analysis revealed that the best CrtM mutants performed comparably to CrtB in an in vivo C40 pathway. These mutants showed significant variation in performance in their original C30 pathway, indicating the emergence of enzymes with broadened substrate specificity as well as those with shifted specificity. We discovered that Phe 26 alone determines the specificity of CrtM. The plasticity of CrtM with respect to its substrate and product range highlights the potential for creating further new carotenoid backbone structures.


FEBS Letters ◽  
1999 ◽  
Vol 460 (2) ◽  
pp. 207-211 ◽  
Author(s):  
Stefanie Bungert ◽  
Bianca Krafft ◽  
Ramona Schlesinger ◽  
Thorsten Friedrich

2006 ◽  
Vol 189 (3) ◽  
pp. 880-885 ◽  
Author(s):  
Jason A. Hall ◽  
Ana M. Pajor

ABSTRACT In Staphylococcus aureus, the transport of dicarboxylates is mediated in part by the Na+-linked carrier protein SdcS. This transporter is a member of the divalent-anion/Na+ symporter (DASS) family, a group that includes the mammalian Na+/dicarboxylate cotransporters NaDC1 and NaDC3. In earlier work, we cloned and expressed SdcS in Escherichia coli and found it to have transport properties similar to those of its eukaryotic counterparts (J. A. Hall and A. M. Pajor, J. Bacteriol. 187:5189-5194, 2005). Here, we report the partial purification and subsequent reconstitution of functional SdcS into liposomes. These proteoliposomes exhibited succinate counterflow activity, as well as Na+ electrochemical-gradient-driven transport. Examination of substrate specificity indicated that the minimal requirement necessary for transport was a four-carbon terminal dicarboxylate backbone and that productive substrate-transporter interaction was sensitive to substitutions at the substrate C-2 and C-3 positions. Further analysis established that SdcS facilitates an electroneutral symport reaction having a 2:1 cation/dicarboxylate ratio. This study represents the first characterization of a reconstituted Na+-coupled DASS family member, thus providing an effective method to evaluate functional, as well as structural, aspects of DASS transporters in a system free of the complexities and constraints associated with native membrane environments.


1994 ◽  
Vol 112 (1) ◽  
pp. 93-101 ◽  
Author(s):  
J. F. Richardson ◽  
P. Aparicio ◽  
R. R. Marples ◽  
B. D. Cookson

SummaryRibotyping, with homologous or heterologous (Escherichia coli) r–RNA, of the propagating strains for phages of the international set for strains ofStaphylococcus aureusof human origin was undertaken to determine the discrimination of this typing method. Ribotyping could distinguish between strains of different phage groups, but could not distinguish between seven phage group III strains of different phage type. Ribotyping may be a useful adjunct to phage typing inS. aureusbut is unlikely to replace it as the primary method of epidemiological typing.


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