Matches in SemOpenAlex for { <https://semopenalex.org/work/W2072493172> ?p ?o ?g. }
Showing items 1 to 87 of
87
with 100 items per page.
- W2072493172 endingPage "3400" @default.
- W2072493172 startingPage "3393" @default.
- W2072493172 abstract "Acetyl-CoA carboxylase catalyzes the first committed step in the biosynthesis of long-chain fatty acids. The Escherichia coli form of the enzyme consists of a biotin carboxylase protein, a biotin carboxyl carrier protein, and a carboxyltransferase protein. In this report a system for site-directed mutagenesis of the biotin carboxylase component is described. The wild-type copy of the enzyme, derived from the chromosomal gene, is separated from the mutant form of the enzyme which is coded on a plasmid. Separation of the two forms is accomplished using a histidine-tag attached to the amino terminus of the mutant form of the enzyme and nickel affinity chromatography. This system was used to mutate four active site residues, E211, E288, N290, and R292, to alanine followed by their characterization with respect to several different reactions catalyzed by biotin carboxylase. In comparison to wild-type biotin carboxylase, all four mutant enzymes gave very similar results in all the different assays, suggesting that the mutated residues have a common function. The mutations did not affect the bicarbonate-dependent ATPase reaction. In contrast, the mutations decreased the maximal velocity of the biotin-dependent ATPase reaction 1000-fold but did not affect the Km for biotin. The activity of the ATP synthesis reaction catalyzed by biotin carboxylase where carbamoyl phosphate reacts with ADP was decreased 100-fold by the mutations. The ATP synthesis reaction required biotin to stimulate the activity in the wild-type; however, biotin did not stimulate the activity of the mutant enzymes. The results showed that the mutations have abolished the ability of biotin to increase the activity of the enzyme. Thus, E211, E288, N290, and R292 were responsible, at least in part, for the substrate-induced synergism by biotin in biotin carboxylase." @default.
- W2072493172 created "2016-06-24" @default.
- W2072493172 creator A5005061229 @default.
- W2072493172 creator A5029991665 @default.
- W2072493172 creator A5030049705 @default.
- W2072493172 creator A5064247860 @default.
- W2072493172 date "1999-02-20" @default.
- W2072493172 modified "2023-09-24" @default.
- W2072493172 title "Mutations at Four Active Site Residues of Biotin Carboxylase Abolish Substrate-Induced Synergism by Biotin" @default.
- W2072493172 cites W1561402256 @default.
- W2072493172 cites W1590008587 @default.
- W2072493172 cites W2056085463 @default.
- W2072493172 cites W2130755410 @default.
- W2072493172 doi "https://doi.org/10.1021/bi982660a" @default.
- W2072493172 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10079084" @default.
- W2072493172 hasPublicationYear "1999" @default.
- W2072493172 type Work @default.
- W2072493172 sameAs 2072493172 @default.
- W2072493172 citedByCount "64" @default.
- W2072493172 countsByYear W20724931722012 @default.
- W2072493172 countsByYear W20724931722013 @default.
- W2072493172 countsByYear W20724931722014 @default.
- W2072493172 countsByYear W20724931722015 @default.
- W2072493172 countsByYear W20724931722016 @default.
- W2072493172 countsByYear W20724931722017 @default.
- W2072493172 countsByYear W20724931722018 @default.
- W2072493172 countsByYear W20724931722019 @default.
- W2072493172 countsByYear W20724931722020 @default.
- W2072493172 countsByYear W20724931722021 @default.
- W2072493172 countsByYear W20724931722022 @default.
- W2072493172 crossrefType "journal-article" @default.
- W2072493172 hasAuthorship W2072493172A5005061229 @default.
- W2072493172 hasAuthorship W2072493172A5029991665 @default.
- W2072493172 hasAuthorship W2072493172A5030049705 @default.
- W2072493172 hasAuthorship W2072493172A5064247860 @default.
- W2072493172 hasConcept C103408237 @default.
- W2072493172 hasConcept C104317684 @default.
- W2072493172 hasConcept C140137476 @default.
- W2072493172 hasConcept C143065580 @default.
- W2072493172 hasConcept C153911025 @default.
- W2072493172 hasConcept C16318435 @default.
- W2072493172 hasConcept C181199279 @default.
- W2072493172 hasConcept C185592680 @default.
- W2072493172 hasConcept C197957613 @default.
- W2072493172 hasConcept C2778204606 @default.
- W2072493172 hasConcept C2779318131 @default.
- W2072493172 hasConcept C2779856020 @default.
- W2072493172 hasConcept C515207424 @default.
- W2072493172 hasConcept C55493867 @default.
- W2072493172 hasConcept C86803240 @default.
- W2072493172 hasConceptScore W2072493172C103408237 @default.
- W2072493172 hasConceptScore W2072493172C104317684 @default.
- W2072493172 hasConceptScore W2072493172C140137476 @default.
- W2072493172 hasConceptScore W2072493172C143065580 @default.
- W2072493172 hasConceptScore W2072493172C153911025 @default.
- W2072493172 hasConceptScore W2072493172C16318435 @default.
- W2072493172 hasConceptScore W2072493172C181199279 @default.
- W2072493172 hasConceptScore W2072493172C185592680 @default.
- W2072493172 hasConceptScore W2072493172C197957613 @default.
- W2072493172 hasConceptScore W2072493172C2778204606 @default.
- W2072493172 hasConceptScore W2072493172C2779318131 @default.
- W2072493172 hasConceptScore W2072493172C2779856020 @default.
- W2072493172 hasConceptScore W2072493172C515207424 @default.
- W2072493172 hasConceptScore W2072493172C55493867 @default.
- W2072493172 hasConceptScore W2072493172C86803240 @default.
- W2072493172 hasIssue "11" @default.
- W2072493172 hasLocation W20724931721 @default.
- W2072493172 hasLocation W20724931722 @default.
- W2072493172 hasOpenAccess W2072493172 @default.
- W2072493172 hasPrimaryLocation W20724931721 @default.
- W2072493172 hasRelatedWork W1484432920 @default.
- W2072493172 hasRelatedWork W1566082825 @default.
- W2072493172 hasRelatedWork W15709554 @default.
- W2072493172 hasRelatedWork W1990614632 @default.
- W2072493172 hasRelatedWork W1991726737 @default.
- W2072493172 hasRelatedWork W2052170108 @default.
- W2072493172 hasRelatedWork W2083773718 @default.
- W2072493172 hasRelatedWork W2092248171 @default.
- W2072493172 hasRelatedWork W2098700683 @default.
- W2072493172 hasRelatedWork W2749590984 @default.
- W2072493172 hasVolume "38" @default.
- W2072493172 isParatext "false" @default.
- W2072493172 isRetracted "false" @default.
- W2072493172 magId "2072493172" @default.
- W2072493172 workType "article" @default.