羟氨苄青霉素引起大疱性类天疱疮样疹

https://www.cell.com/molecular-plant/pdf/S1674-2052(15)00366-4.pdf

Amino Acid Catabolism in Plants

http://sgpwe.izt.uam.mx/files/users/uami/sho/Hult2007_Enzyme_promiscuity_mechanism_and_applications.pdf

Enzyme promiscuity : mechanism and applications

Because bisphenol A (BPA) is a high production volume chemical, we examined over 500 peer-reviewed studies to understand its global distribution in effluent discharges, surface waters, sewage sludge, biosolids, sediments, soils, air, wildlife, and humans. Bisphenol A was largely reported from urban ecosystems in Asia, Europe, and North America; unfortunately, information was lacking from large geographic areas, megacities, and developing countries. When sufficient data were available, probabilistic hazard assessments were performed to understand global environmental quality concerns. Exceedances of Canadian Predicted No Effect Concentrations for aquatic life were >50% for effluents in Asia, Europe, and North America but as high as 80% for surface water reports from Asia. Similarly, maximum concentrations of BPA in sediments from Asia were higher than Europe. Concentrations of BPA in wildlife, mostly for fish, ranged from 0.2 to 13 000 ng/g. We observed 60% and 40% exceedences of median levels by the US Centers for Disease Control and Prevention's National Health and Nutrition Examination Survey in Europe and Asia, respectively. These findings highlight the utility of coordinating global sensing of environmental contaminants efforts through integration of environmental monitoring and specimen banking to identify regions for implementation of more robust environmental assessment and management programs.

https://journals.sagepub.com/doi/pdf/10.1177/1559325815598308

Global Assessment of Bisphenol A in the Environment Review and Analysis of Its Occurrence and Bioaccumulation

Herein we review recent advances in the asymmetric reduction of ketones by biocatalysts. Included are discussions on recent developments in methodologies to control enantioselectivities of catalytic reactions, and examples of practical applications that reduce various types of ketones are also shown.

Recent developments in asymmetric reduction of ketones with biocatalysts

Stereochemical control of microbial reduction. 17. A method for controlling the enantioselectivity of reductions with bakers' yeast

Stable and potent fibrinolytic enzymes (six homogeneous proteins) were purified to homogeneity from extracts of the lyophilized powder of an earthworm, Lumbricus rubellus. The molecular weight of each enzyme estimated by SDS-polyacrylamide gel electrophoresis was different from those by gel filtration chromatography in the six purified proteins. The exact molecular weight of each enzyme (F-III-2, F-III-1, F-II, F-I-2, F-I-1, and F-I-0) measured by ion-spray MS analysis was 29,662, 29,667, 24,664, 24,220, 24,196, and 23,013, respectively. The isoelectric point (pI) of each enzyme was 3.40, 3.60, 4.20, 4.00, 4.30, and 4.85, respectively. The enzymes were single polypeptide chains. They had a very strong fibrinolytic activity and the maximum reactivity for chromogenic substrates from pH 9-11. The enzymes, acidic proteins that had abundant asparagine and aspartic acid, and low lysine in their amino acid composition, did not contain component sugars. The enzymes were stable at from pH 1-11 and up to 60 degrees C. Studies on substrate specificity and inhibition indicated that these enzymes were alkaline trypsin-like serine proteases. N-Terminal amino acid sequences of the enzymes had local similarities to those of trypsin-like enzymes such as elastase and coagulation factor IX. From the results of amino acid sequence, amino acid composition analyses and immunological analyses, it was suggested that these six enzyme proteins were derived as isozyme(s) from at least four different genes.

Characterization of Potent Fibrinolytic Enzymes in Earthworm, Lumbricus rubellus

Enhancement of water-solubility and bioactivity of paclitaxel using modified cyclodextrins

Biotransformation of thymol, carvacrol, and eugenol by cultured cells of Eucalyptus perriniana.

Katsuwokinase (KK) is a unique fibrinolytic enzyme recently found in skipjack “Shiokara” a Japanese traditional salt-fermented food. A crude enzyme extracted from skipjack Shiokara ( Katsuwonus pelamis ) showed a very strong fibrinolytic activity above 45 CU/g (fibrin plate method) based on plasmin. KK not only hydrolyzed fibrin but also several synthetic amido substrates, particularly pyro-Glu-Gly-Arg-pNA. The fibrinolytic activity of KK was not affected in the presence of 10% NaCl, was stable in the pH range from 1 to 10 at 37°C for 30 min, and was inhibited by DFP, SBTI, BPTI, and aprotinin but not by e-amino-n-caproic acid and t-4-amino-methylcyclohexane carboxylic acid. The crude enzyme contained at least four kinds of KK, and the major form purified had a pI value of -5.0 and a molecular weight of 35,000. The N-terminal amino acid sequence of 21 residues, I-V-G-G-Y-E-Q-Z-A-H-S-Q-P-H-Q-V-S-L-N-S-G-, had 80 % homology with that of trypsin. The fibrinolytic activity of the purified enzyme was -2.6 times greater than that of plasmin by molar ratio, demonstrating its identity as a new and very potent fibrinolytic enzyme.

Nobuyoshi Nakajima

Papers

Stereochemical control of microbial reduction. 17. A method for controlling the enantioselectivity of reductions with bakers' yeast

Characterization of Potent Fibrinolytic Enzymes in Earthworm, Lumbricus rubellus

Enhancement of water-solubility and bioactivity of paclitaxel using modified cyclodextrins

Biotransformation of thymol, carvacrol, and eugenol by cultured cells of Eucalyptus perriniana.

A unique strong fibrinolytic enzyme (katsuwokinase) in skipjack “Shiokara” a Japanese traditional fermented food