FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2032000289> ?p ?o ?g. }

• W2032000289 endingPage "813" @default.
• W2032000289 startingPage "804" @default.
• W2032000289 abstract "Aflatoxin B1 is a potent environmental carcinogen produced by certain strains of Aspergillus. Central to the biosynthesis of this mycotoxin is the reaction catalyzed by versicolorin B synthase (VBS) in which a racemic substrate, versiconal hemiacetal, is cyclized to an optically active product whose absolute configuration is crucial to the interaction of aflatoxin B1 with DNA. Attempted over-production of VBS in Escherichia coli led principally to protein aggregated into inclusion bodies but also small amounts of soluble but catalytically inactive enzyme. Comparisons to wild-type VBS by SDS-polyacrylamide gel electrophoresis and after N-glycosidase F treatment revealed that extensive glycosylation accounted for the mass discrepancy (7,000 ±; 1,500 Da) between the native and bacterially expressed proteins. Several over-expression systems in Saccharomyces cerevisiae were surveyed in which one that incorporated a secretion signal was found most successful. VBS of indistinguishable mass on SDS-polyacrylamide gel electrophoresis and kinetic properties from the wild-type enzyme could be obtained in 50-100-fold greater amounts and whose catalytic behavior has been examined. The translated protein sequence of VBS showed three potential N-glycosylation sites (Asn-Xaa-Ser/Thr) consistent with the modifications observed above and unexpectedly revealed extensive homology to the ADP-binding region prominently conserved in the glucose-methanol-choline (GMC) family of flavoenzymes. Over-production of VBS in yeast marks the first aflatoxin biosynthetic enzyme to be so obtained and opens the way to direct study of the enzymology of this complex biosynthetic pathway. Aflatoxin B1 is a potent environmental carcinogen produced by certain strains of Aspergillus. Central to the biosynthesis of this mycotoxin is the reaction catalyzed by versicolorin B synthase (VBS) in which a racemic substrate, versiconal hemiacetal, is cyclized to an optically active product whose absolute configuration is crucial to the interaction of aflatoxin B1 with DNA. Attempted over-production of VBS in Escherichia coli led principally to protein aggregated into inclusion bodies but also small amounts of soluble but catalytically inactive enzyme. Comparisons to wild-type VBS by SDS-polyacrylamide gel electrophoresis and after N-glycosidase F treatment revealed that extensive glycosylation accounted for the mass discrepancy (7,000 ±; 1,500 Da) between the native and bacterially expressed proteins. Several over-expression systems in Saccharomyces cerevisiae were surveyed in which one that incorporated a secretion signal was found most successful. VBS of indistinguishable mass on SDS-polyacrylamide gel electrophoresis and kinetic properties from the wild-type enzyme could be obtained in 50-100-fold greater amounts and whose catalytic behavior has been examined. The translated protein sequence of VBS showed three potential N-glycosylation sites (Asn-Xaa-Ser/Thr) consistent with the modifications observed above and unexpectedly revealed extensive homology to the ADP-binding region prominently conserved in the glucose-methanol-choline (GMC) family of flavoenzymes. Over-production of VBS in yeast marks the first aflatoxin biosynthetic enzyme to be so obtained and opens the way to direct study of the enzymology of this complex biosynthetic pathway." @default.
• W2032000289 created "2016-06-24" @default.
• W2032000289 creator A5016503420 @default.
• W2032000289 creator A5067252545 @default.
• W2032000289 date "1997-01-01" @default.
• W2032000289 modified "2023-10-07" @default.
• W2032000289 title "Heterologous Expression, Isolation, and Characterization of Versicolorin B Synthase from Aspergillus parasiticus" @default.
• W2032000289 cites W1164428528 @default.
• W2032000289 cites W1484425045 @default.
• W2032000289 cites W1501627837 @default.
• W2032000289 cites W1501687440 @default.
• W2032000289 cites W1508204777 @default.
• W2032000289 cites W1548897436 @default.
• W2032000289 cites W1596367871 @default.
• W2032000289 cites W1668945774 @default.
• W2032000289 cites W1806791563 @default.
• W2032000289 cites W1930403958 @default.
• W2032000289 cites W1966509393 @default.
• W2032000289 cites W1966611807 @default.
• W2032000289 cites W1968807472 @default.
• W2032000289 cites W1969009853 @default.
• W2032000289 cites W1969696437 @default.
• W2032000289 cites W1972787114 @default.
• W2032000289 cites W1975412754 @default.
• W2032000289 cites W1981116520 @default.
• W2032000289 cites W1990928842 @default.
• W2032000289 cites W1992154269 @default.
• W2032000289 cites W1997517589 @default.
• W2032000289 cites W2001019297 @default.
• W2032000289 cites W2004842433 @default.
• W2032000289 cites W2006762876 @default.
• W2032000289 cites W2007677383 @default.
• W2032000289 cites W2017102544 @default.
• W2032000289 cites W2021388735 @default.
• W2032000289 cites W2022016707 @default.
• W2032000289 cites W2022284358 @default.
• W2032000289 cites W2025175775 @default.
• W2032000289 cites W2031119708 @default.
• W2032000289 cites W2032606624 @default.
• W2032000289 cites W2033932745 @default.
• W2032000289 cites W2042316019 @default.
• W2032000289 cites W2046153401 @default.
• W2032000289 cites W2055319465 @default.
• W2032000289 cites W2058288184 @default.
• W2032000289 cites W2068518785 @default.
• W2032000289 cites W2079309779 @default.
• W2032000289 cites W2081446575 @default.
• W2032000289 cites W2092057183 @default.
• W2032000289 cites W2100837269 @default.
• W2032000289 cites W2106706022 @default.
• W2032000289 cites W2113138690 @default.
• W2032000289 cites W2115045203 @default.
• W2032000289 cites W2123738381 @default.
• W2032000289 cites W2130040066 @default.
• W2032000289 cites W2134266321 @default.
• W2032000289 cites W2136451426 @default.
• W2032000289 cites W2139559115 @default.
• W2032000289 cites W2150111409 @default.
• W2032000289 cites W2150819625 @default.
• W2032000289 cites W2158449128 @default.
• W2032000289 cites W2165950552 @default.
• W2032000289 cites W2335671215 @default.
• W2032000289 cites W2341209396 @default.
• W2032000289 cites W2405173083 @default.
• W2032000289 cites W2462232898 @default.
• W2032000289 cites W2950469006 @default.
• W2032000289 cites W2969273703 @default.
• W2032000289 cites W3098125447 @default.
• W2032000289 cites W4250353074 @default.
• W2032000289 cites W4293247451 @default.
• W2032000289 cites W955725593 @default.
• W2032000289 doi "https://doi.org/10.1074/jbc.272.2.804" @default.
• W2032000289 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8995367" @default.
• W2032000289 hasPublicationYear "1997" @default.
• W2032000289 type Work @default.
• W2032000289 sameAs 2032000289 @default.
• W2032000289 citedByCount "24" @default.
• W2032000289 countsByYear W20320002892012 @default.
• W2032000289 countsByYear W20320002892013 @default.
• W2032000289 countsByYear W20320002892014 @default.
• W2032000289 countsByYear W20320002892017 @default.
• W2032000289 countsByYear W20320002892018 @default.
• W2032000289 countsByYear W20320002892019 @default.
• W2032000289 countsByYear W20320002892020 @default.
• W2032000289 countsByYear W20320002892021 @default.
• W2032000289 countsByYear W20320002892022 @default.
• W2032000289 crossrefType "journal-article" @default.
• W2032000289 hasAuthorship W2032000289A5016503420 @default.
• W2032000289 hasAuthorship W2032000289A5067252545 @default.
• W2032000289 hasBestOaLocation W20320002891 @default.
• W2032000289 hasConcept C101660505 @default.
• W2032000289 hasConcept C103432212 @default.
• W2032000289 hasConcept C181199279 @default.
• W2032000289 hasConcept C185592680 @default.
• W2032000289 hasConcept C2776390506 @default.
• W2032000289 hasConcept C2777292910 @default.
• W2032000289 hasConcept C2777313579 @default.
• W2032000289 hasConcept C553450214 @default.

• next