FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2013828401> ?p ?o ?g. }

• W2013828401 endingPage "2887" @default.
• W2013828401 startingPage "2874" @default.
• W2013828401 abstract "The anaerobic sulfatase-maturating enzyme from Clostridium perfringens (anSMEcpe) catalyzes the two-electron oxidation of a cysteinyl residue on a cognate protein to a formylglycyl residue (FGly) using a mechanism that involves organic radicals. The FGly residue plays a unique role as a cofactor in a class of enzymes termed arylsulfatases, which catalyze the hydrolysis of various organosulfate monoesters. anSMEcpe has been shown to be a member of the radical S-adenosylmethionine (SAM) family of enzymes, [4Fe-4S] cluster-requiring proteins that use a 5'-deoxyadenosyl 5'-radical (5'-dA(•)) generated from a reductive cleavage of SAM to initiate radical-based catalysis. Herein, we show that anSMEcpe contains in addition to the [4Fe-4S] cluster harbored by all radical SAM (RS) enzymes, two additional [4Fe-4S] clusters, similar to the radical SAM protein AtsB, which catalyzes the two-electron oxidation of a seryl residue to a FGly residue. We show by size-exclusion chromatography that both AtsB and anSMEcpe are monomeric proteins, and site-directed mutagenesis studies of AtsB reveal that individual Cys → Ala substitutions at seven conserved positions result in an insoluble protein, consistent with those residues acting as ligands to the two additional [4Fe-4S] clusters. Ala substitutions at an additional conserved Cys residue (C291 in AtsB and C276 in anSMEcpe) afford proteins that display intermediate behavior. These proteins exhibit reduced solubility and drastically reduced activity, behavior that is conspicuously similar to that of a critical Cys residue in BtrN, another radical SAM dehydrogenase [Grove, T. L., et al. (2010) Biochemistry 49, 3783-3785]. We also show that wild-type anSMEcpe acts on peptides containing other oxidizable amino acids at the target position. Moreover, we show that the enzyme will convert threonyl peptides to the corresponding ketone product, and also allo-threonyl peptides, but with a significantly reduced efficiency, suggesting that the pro-S hydrogen atom of the normal cysteinyl substrate is stereoselectively removed during turnover. Lastly, we show that the electron generated during catalysis by AtsB and anSMEcpe can be utilized for multiple turnovers, albeit through a reduced flavodoxin-mediated pathway." @default.
• W2013828401 created "2016-06-24" @default.
• W2013828401 creator A5033223684 @default.
• W2013828401 creator A5043759221 @default.
• W2013828401 creator A5045998043 @default.
• W2013828401 creator A5050467129 @default.
• W2013828401 creator A5055149042 @default.
• W2013828401 creator A5058295442 @default.
• W2013828401 creator A5072945047 @default.
• W2013828401 date "2013-04-16" @default.
• W2013828401 modified "2023-10-18" @default.
• W2013828401 title "Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in the Mechanism of Catalysis" @default.
• W2013828401 cites W1000442924 @default.
• W2013828401 cites W1578537067 @default.
• W2013828401 cites W1745490809 @default.
• W2013828401 cites W1970221770 @default.
• W2013828401 cites W1970855127 @default.
• W2013828401 cites W1975967012 @default.
• W2013828401 cites W1976007598 @default.
• W2013828401 cites W1976325156 @default.
• W2013828401 cites W1976359573 @default.
• W2013828401 cites W1976488653 @default.
• W2013828401 cites W1979280203 @default.
• W2013828401 cites W1985652038 @default.
• W2013828401 cites W1985710061 @default.
• W2013828401 cites W1985770761 @default.
• W2013828401 cites W2001521415 @default.
• W2013828401 cites W2004939146 @default.
• W2013828401 cites W2007093553 @default.
• W2013828401 cites W2007796873 @default.
• W2013828401 cites W2013248441 @default.
• W2013828401 cites W2017241270 @default.
• W2013828401 cites W2017339825 @default.
• W2013828401 cites W2021804555 @default.
• W2013828401 cites W2029120628 @default.
• W2013828401 cites W2029539382 @default.
• W2013828401 cites W2030143932 @default.
• W2013828401 cites W2038723018 @default.
• W2013828401 cites W2043330551 @default.
• W2013828401 cites W2044608069 @default.
• W2013828401 cites W2050117377 @default.
• W2013828401 cites W2054905327 @default.
• W2013828401 cites W2056108846 @default.
• W2013828401 cites W2059133046 @default.
• W2013828401 cites W2062920334 @default.
• W2013828401 cites W2069479627 @default.
• W2013828401 cites W2069748244 @default.
• W2013828401 cites W2072062484 @default.
• W2013828401 cites W2072471477 @default.
• W2013828401 cites W2075040966 @default.
• W2013828401 cites W2081124607 @default.
• W2013828401 cites W2081474793 @default.
• W2013828401 cites W2083921257 @default.
• W2013828401 cites W2084182165 @default.
• W2013828401 cites W2084744164 @default.
• W2013828401 cites W2086003789 @default.
• W2013828401 cites W2087875520 @default.
• W2013828401 cites W2093094655 @default.
• W2013828401 cites W2097589722 @default.
• W2013828401 cites W2107789695 @default.
• W2013828401 cites W2110506044 @default.
• W2013828401 cites W2131032705 @default.
• W2013828401 cites W2143351258 @default.
• W2013828401 cites W2149189957 @default.
• W2013828401 cites W2152707194 @default.
• W2013828401 cites W2317135731 @default.
• W2013828401 cites W2410339214 @default.
• W2013828401 cites W4211083314 @default.
• W2013828401 cites W4211206272 @default.
• W2013828401 cites W4293247451 @default.
• W2013828401 doi "https://doi.org/10.1021/bi400136u" @default.
• W2013828401 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3897223" @default.
• W2013828401 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23477283" @default.
• W2013828401 hasPublicationYear "2013" @default.
• W2013828401 type Work @default.
• W2013828401 sameAs 2013828401 @default.
• W2013828401 citedByCount "52" @default.
• W2013828401 countsByYear W20138284012013 @default.
• W2013828401 countsByYear W20138284012014 @default.
• W2013828401 countsByYear W20138284012015 @default.
• W2013828401 countsByYear W20138284012016 @default.
• W2013828401 countsByYear W20138284012017 @default.
• W2013828401 countsByYear W20138284012018 @default.
• W2013828401 countsByYear W20138284012019 @default.
• W2013828401 countsByYear W20138284012020 @default.
• W2013828401 countsByYear W20138284012021 @default.
• W2013828401 countsByYear W20138284012022 @default.
• W2013828401 countsByYear W20138284012023 @default.
• W2013828401 crossrefType "journal-article" @default.
• W2013828401 hasAuthorship W2013828401A5033223684 @default.
• W2013828401 hasAuthorship W2013828401A5043759221 @default.
• W2013828401 hasAuthorship W2013828401A5045998043 @default.
• W2013828401 hasAuthorship W2013828401A5050467129 @default.
• W2013828401 hasAuthorship W2013828401A5055149042 @default.
• W2013828401 hasAuthorship W2013828401A5058295442 @default.
• W2013828401 hasAuthorship W2013828401A5072945047 @default.
• W2013828401 hasBestOaLocation W20138284012 @default.
• W2013828401 hasConcept C181199279 @default.

• next