FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1583600599> ?p ?o ?g. }

• W1583600599 endingPage "3501" @default.
• W1583600599 startingPage "3496" @default.
• W1583600599 abstract "Affinity labeling and comparative sequence analyses have placed Lys-166 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at the active site. The unusual nucleophilicity and acidity of the epsilon-amino group of Lys 166 (pKa = 7.9) suggest its involvement in catalysis, perhaps as the base that enolizes ribulosebisphosphate (Hartman, F.C., Milanez, S., and Lee, E.H. (1985) J. Biol. Chem. 260, 13968-13975). In attempts to clarify the role of Lys-166 of the carboxylase, we have used site-directed mutagenesis to replace this lysyl residue with glycine, alanine, serine, glutamine, arginine, cysteine, or histidine. All seven of these mutant proteins, purified by immunoaffinity chromatography, are severely deficient in carboxylase activity; the serine mutant, which is the most active, has a kcat only 0.2% that of the wild-type enzyme. Although low, the carboxylase activity displayed by some of the mutant proteins proves that Lys-166 is not required for substrate binding and argues that the detrimental effects brought about by amino acid substitutions at position 166 do not reflect gross conformational changes. As demonstrated by their ability to tightly bind a transition-state analogue (2-carboxyarabinitol 1,5-bisphosphate) in the presence of CO2 and Mg2+, some of the mutant proteins undergo the carbamylation reaction that is required for activation of the wild-type enzyme. Since Lys-166 is required neither for activation (i.e. carbamylation by CO2) nor for substrate binding, it must be essential to catalysis. When viewed within the context of previous related studies, the results of site-directed mutagenesis are entirely consistent with Lys-166 functioning as the base that initiates catalysis by abstracting the C-3 proton from ribulosebisphosphate. An alternative possibility that Lys-166 acts to stabilize a transition state in the reaction pathway cannot be rigorously excluded." @default.
• W1583600599 created "2016-06-24" @default.
• W1583600599 creator A5013149126 @default.
• W1583600599 creator A5013563881 @default.
• W1583600599 creator A5021868057 @default.
• W1583600599 creator A5028712723 @default.
• W1583600599 creator A5044941103 @default.
• W1583600599 creator A5061492568 @default.
• W1583600599 creator A5068140875 @default.
• W1583600599 creator A5082029120 @default.
• W1583600599 creator A5085691586 @default.
• W1583600599 date "1987-03-01" @default.
• W1583600599 modified "2023-09-28" @default.
• W1583600599 title "Function of Lys-166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase as examined by site-directed mutagenesis." @default.
• W1583600599 cites W1485271133 @default.
• W1583600599 cites W1486212748 @default.
• W1583600599 cites W1500386244 @default.
• W1583600599 cites W1538114820 @default.
• W1583600599 cites W1587613188 @default.
• W1583600599 cites W1969073425 @default.
• W1583600599 cites W1975304761 @default.
• W1583600599 cites W1976566308 @default.
• W1583600599 cites W1978754461 @default.
• W1583600599 cites W1983435526 @default.
• W1583600599 cites W1984010866 @default.
• W1583600599 cites W1984217527 @default.
• W1583600599 cites W1984286262 @default.
• W1583600599 cites W1992368067 @default.
• W1583600599 cites W1995312935 @default.
• W1583600599 cites W1999292449 @default.
• W1583600599 cites W1999629473 @default.
• W1583600599 cites W2016996689 @default.
• W1583600599 cites W2018374847 @default.
• W1583600599 cites W2019853549 @default.
• W1583600599 cites W2025450446 @default.
• W1583600599 cites W2028220139 @default.
• W1583600599 cites W2028622989 @default.
• W1583600599 cites W2040991518 @default.
• W1583600599 cites W2044952215 @default.
• W1583600599 cites W2058533791 @default.
• W1583600599 cites W2059641706 @default.
• W1583600599 cites W2060117087 @default.
• W1583600599 cites W2074778021 @default.
• W1583600599 cites W2079388890 @default.
• W1583600599 cites W2085162051 @default.
• W1583600599 cites W2092255043 @default.
• W1583600599 cites W2092386497 @default.
• W1583600599 cites W2094201919 @default.
• W1583600599 cites W2100837269 @default.
• W1583600599 cites W2127400370 @default.
• W1583600599 cites W2138270253 @default.
• W1583600599 cites W2169880108 @default.
• W1583600599 cites W2170986838 @default.
• W1583600599 cites W2180256823 @default.
• W1583600599 cites W2285904922 @default.
• W1583600599 cites W2745627398 @default.
• W1583600599 cites W333539686 @default.
• W1583600599 cites W4293247451 @default.
• W1583600599 doi "https://doi.org/10.1016/s0021-9258(18)61378-x" @default.
• W1583600599 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3102487" @default.
• W1583600599 hasPublicationYear "1987" @default.
• W1583600599 type Work @default.
• W1583600599 sameAs 1583600599 @default.
• W1583600599 citedByCount "56" @default.
• W1583600599 countsByYear W15836005992019 @default.
• W1583600599 countsByYear W15836005992020 @default.
• W1583600599 countsByYear W15836005992023 @default.
• W1583600599 crossrefType "journal-article" @default.
• W1583600599 hasAuthorship W1583600599A5013149126 @default.
• W1583600599 hasAuthorship W1583600599A5013563881 @default.
• W1583600599 hasAuthorship W1583600599A5021868057 @default.
• W1583600599 hasAuthorship W1583600599A5028712723 @default.
• W1583600599 hasAuthorship W1583600599A5044941103 @default.
• W1583600599 hasAuthorship W1583600599A5061492568 @default.
• W1583600599 hasAuthorship W1583600599A5068140875 @default.
• W1583600599 hasAuthorship W1583600599A5082029120 @default.
• W1583600599 hasAuthorship W1583600599A5085691586 @default.
• W1583600599 hasBestOaLocation W15836005991 @default.
• W1583600599 hasConcept C103408237 @default.
• W1583600599 hasConcept C104317684 @default.
• W1583600599 hasConcept C140137476 @default.
• W1583600599 hasConcept C14036430 @default.
• W1583600599 hasConcept C143065580 @default.
• W1583600599 hasConcept C16318435 @default.
• W1583600599 hasConcept C165474305 @default.
• W1583600599 hasConcept C181199279 @default.
• W1583600599 hasConcept C183688256 @default.
• W1583600599 hasConcept C185592680 @default.
• W1583600599 hasConcept C2777082638 @default.
• W1583600599 hasConcept C501734568 @default.
• W1583600599 hasConcept C50212798 @default.
• W1583600599 hasConcept C54355233 @default.
• W1583600599 hasConcept C55493867 @default.
• W1583600599 hasConcept C86803240 @default.
• W1583600599 hasConceptScore W1583600599C103408237 @default.
• W1583600599 hasConceptScore W1583600599C104317684 @default.
• W1583600599 hasConceptScore W1583600599C140137476 @default.
• W1583600599 hasConceptScore W1583600599C14036430 @default.

• next