Matches in SemOpenAlex for { <https://semopenalex.org/work/W2040222784> ?p ?o ?g. }
Showing items 1 to 88 of
88
with 100 items per page.
- W2040222784 endingPage "1222" @default.
- W2040222784 startingPage "1213" @default.
- W2040222784 abstract "The vitamin B6-dependent enzyme 7,8-diaminopelargonic acid (DAPA) synthase catalyzes the antepenultimate step in the synthesis of biotin, the transfer of the α-amino group of S-adenosyl-l-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form DAPA. The Y17F, Y144F, and D147N mutations in the active site were constructed independently. The kmax/Kmapp values for the half-reaction with DAPA of the Y17F and Y144F mutants are reduced by 1300- and 2900-fold, respectively, compared to the WT enzyme. Crystallographic analyses of these mutants do not show significant changes in the structure of the active site. The kinetic deficiencies, together with a structural model of the enzyme-PLP/DAPA Michaelis complex, point to a role of these two residues in recognition of the DAPA/KAPA substrates and in catalysis. The kmax/Kmapp values for the half-reaction with SAM are similar to that of the WT enzyme, showing that the two tyrosine residues are not involved in this half-reaction. Mutations of the conserved Arg253 uniquely affect the SAM kinetics, thus establishing this position as part of the SAM binding site. The D147N mutant is catalytically inactive in both half-reactions. The structure of this mutant exhibits significant changes in the active site, indicating that this residue plays an important structural role. Of the four residues examined, only Tyr144 and Arg253 are strictly conserved in the available amino acid sequences of DAPA synthases. This enzyme thus provides an illustrative example that active site residues essential for catalysis are not necessarily conserved, i.e., that during evolution alternative solutions for efficient catalysis by the same enzyme arose. Decarboxylated SAM [S-adenosyl-(5‘)-3-methylthiopropylamine] reacts nearly as well as SAM and cannot be eliminated as a putative in vivo amino donor." @default.
- W2040222784 created "2016-06-24" @default.
- W2040222784 creator A5010549483 @default.
- W2040222784 creator A5056210872 @default.
- W2040222784 creator A5074102837 @default.
- W2040222784 creator A5077016752 @default.
- W2040222784 creator A5091578401 @default.
- W2040222784 date "2004-01-13" @default.
- W2040222784 modified "2023-10-16" @default.
- W2040222784 title "Conserved and Nonconserved Residues in the Substrate Binding Site of 7,8-Diaminopelargonic Acid Synthase from <i>Escherichia coli</i> Are Essential for Catalysis" @default.
- W2040222784 cites W1484018558 @default.
- W2040222784 cites W1981489012 @default.
- W2040222784 cites W1986191025 @default.
- W2040222784 cites W1999728411 @default.
- W2040222784 cites W2000403981 @default.
- W2040222784 cites W2003300391 @default.
- W2040222784 cites W2060671052 @default.
- W2040222784 cites W2332824477 @default.
- W2040222784 doi "https://doi.org/10.1021/bi0358059" @default.
- W2040222784 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14756557" @default.
- W2040222784 hasPublicationYear "2004" @default.
- W2040222784 type Work @default.
- W2040222784 sameAs 2040222784 @default.
- W2040222784 citedByCount "17" @default.
- W2040222784 countsByYear W20402227842012 @default.
- W2040222784 countsByYear W20402227842015 @default.
- W2040222784 countsByYear W20402227842016 @default.
- W2040222784 countsByYear W20402227842018 @default.
- W2040222784 countsByYear W20402227842020 @default.
- W2040222784 countsByYear W20402227842022 @default.
- W2040222784 crossrefType "journal-article" @default.
- W2040222784 hasAuthorship W2040222784A5010549483 @default.
- W2040222784 hasAuthorship W2040222784A5056210872 @default.
- W2040222784 hasAuthorship W2040222784A5074102837 @default.
- W2040222784 hasAuthorship W2040222784A5077016752 @default.
- W2040222784 hasAuthorship W2040222784A5091578401 @default.
- W2040222784 hasConcept C104317684 @default.
- W2040222784 hasConcept C107824862 @default.
- W2040222784 hasConcept C143065580 @default.
- W2040222784 hasConcept C181199279 @default.
- W2040222784 hasConcept C185592680 @default.
- W2040222784 hasConcept C2776016237 @default.
- W2040222784 hasConcept C2776165026 @default.
- W2040222784 hasConcept C2781338088 @default.
- W2040222784 hasConcept C41183919 @default.
- W2040222784 hasConcept C515207424 @default.
- W2040222784 hasConcept C547475151 @default.
- W2040222784 hasConcept C55493867 @default.
- W2040222784 hasConcept C56856141 @default.
- W2040222784 hasConcept C69118441 @default.
- W2040222784 hasConcept C71240020 @default.
- W2040222784 hasConceptScore W2040222784C104317684 @default.
- W2040222784 hasConceptScore W2040222784C107824862 @default.
- W2040222784 hasConceptScore W2040222784C143065580 @default.
- W2040222784 hasConceptScore W2040222784C181199279 @default.
- W2040222784 hasConceptScore W2040222784C185592680 @default.
- W2040222784 hasConceptScore W2040222784C2776016237 @default.
- W2040222784 hasConceptScore W2040222784C2776165026 @default.
- W2040222784 hasConceptScore W2040222784C2781338088 @default.
- W2040222784 hasConceptScore W2040222784C41183919 @default.
- W2040222784 hasConceptScore W2040222784C515207424 @default.
- W2040222784 hasConceptScore W2040222784C547475151 @default.
- W2040222784 hasConceptScore W2040222784C55493867 @default.
- W2040222784 hasConceptScore W2040222784C56856141 @default.
- W2040222784 hasConceptScore W2040222784C69118441 @default.
- W2040222784 hasConceptScore W2040222784C71240020 @default.
- W2040222784 hasIssue "5" @default.
- W2040222784 hasLocation W20402227841 @default.
- W2040222784 hasLocation W20402227842 @default.
- W2040222784 hasOpenAccess W2040222784 @default.
- W2040222784 hasPrimaryLocation W20402227841 @default.
- W2040222784 hasRelatedWork W1572120979 @default.
- W2040222784 hasRelatedWork W2006946696 @default.
- W2040222784 hasRelatedWork W2010563998 @default.
- W2040222784 hasRelatedWork W2019576136 @default.
- W2040222784 hasRelatedWork W2025398173 @default.
- W2040222784 hasRelatedWork W2040119364 @default.
- W2040222784 hasRelatedWork W2047434710 @default.
- W2040222784 hasRelatedWork W2051291172 @default.
- W2040222784 hasRelatedWork W2052862209 @default.
- W2040222784 hasRelatedWork W2437348584 @default.
- W2040222784 hasVolume "43" @default.
- W2040222784 isParatext "false" @default.
- W2040222784 isRetracted "false" @default.
- W2040222784 magId "2040222784" @default.
- W2040222784 workType "article" @default.