FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2065431624> ?p ?o ?g. }

• W2065431624 endingPage "739" @default.
• W2065431624 startingPage "727" @default.
• W2065431624 abstract "Abstract S-Adenosylmethionine synthetase (MAT, ATP:L-methionine S-adenosyltransferase, E.C.2.5.1.6.) plays a central metabolic role in all organisms. MAT catalyzes the two-step reaction which synthesizes S-adenosylmethionine (AdoMet), pyrophosphate (PPi) and orthophosphate (Pi) from ATP and L-methionine. AdoMet is the primary methyl group donor in biological systems. MAT from Escherichia coli was crystallized in the tetragonal modification with space group P43212 using the same conditions as previously yielded crystals of the hexagonal system [Takusagawa, et al., (1996), J. Biol. Chem., 171, 136–147], except for the crystallization temperature. The structure has been determined by molecular replacement at 3.2 Å resolution. The overall structure of the tetrameric MAT in the tetragonal modification is essentially the same as the structure found in the hexagonal modification. However there are two remarkable differences between the structures of two modifications. One is the contents in the active sites (holo-form vs. apo-form), and the other is the conformation of the flexible loop over the active site (open vs. closed). These differences in the crystal structures are caused solely by the difference in crystallization temperatures (26° C vs. 4° C). We have interpreted the structural data obtained from the X-ray analyses in conjunction with the results of the mechanistic and sequencing studies in terms of possible dynamic motion of the flexible loop. When a substrate/product binds in the active site (hexagonal modification), the loop becomes disordered, apparently due to flexibility at the entrance of the active site as if it acts as a “mobile loop” during the catalytic reaction. On the other hand, when the temperature is decreased, the dynamic motion of the flexible loop may be reduced, and the loop residues enter the active site and close its entrance (tetragonal modification). Thus, the active site of the tetragonal modification is empty despite the crystals being grown in mother liquor containing a large concentration of phosphate (100 mM). There is no significant displacement of amino acid residues in the active site between the holo and apo forms, suggesting that the flexible loop plays an important role in determination of the contents in the active site. Since the functionally important amino acid residues in the active site are all conserved throughout various species, the structures of the active sites and the mechanism of the catalysis are probably essentially identical in the enzymes from a wide range of organisms. However, the substrate K m and Vmax values of MATs from various species are distributed over a wide range. The amino acid residues in the flexible loop regions are poorly conserved throughout various species. Therefore, the wide differences in catalysis rates of MATs from various species may be due to the differences in the composition of the flexible loop." @default.
• W2065431624 created "2016-06-24" @default.
• W2065431624 creator A5026933296 @default.
• W2065431624 creator A5045061541 @default.
• W2065431624 creator A5064890753 @default.
• W2065431624 creator A5068337005 @default.
• W2065431624 date "1996-04-01" @default.
• W2065431624 modified "2023-10-17" @default.
• W2065431624 title "Flexible Loop in the Structure of S-Adenosylmethionine Synthetase Crystallized in the Tetragonal Modification" @default.
• W2065431624 cites W1494198800 @default.
• W2065431624 cites W1528355938 @default.
• W2065431624 cites W1562187797 @default.
• W2065431624 cites W1569652852 @default.
• W2065431624 cites W1570435661 @default.
• W2065431624 cites W1578409044 @default.
• W2065431624 cites W1589981507 @default.
• W2065431624 cites W1771251144 @default.
• W2065431624 cites W1838617752 @default.
• W2065431624 cites W1898770275 @default.
• W2065431624 cites W1967503480 @default.
• W2065431624 cites W1973453628 @default.
• W2065431624 cites W1976729123 @default.
• W2065431624 cites W1983753605 @default.
• W2065431624 cites W1987814777 @default.
• W2065431624 cites W1990394926 @default.
• W2065431624 cites W1996607909 @default.
• W2065431624 cites W2004370807 @default.
• W2065431624 cites W2009310436 @default.
• W2065431624 cites W2014405390 @default.
• W2065431624 cites W2015619491 @default.
• W2065431624 cites W2018712761 @default.
• W2065431624 cites W2033343909 @default.
• W2065431624 cites W2038711991 @default.
• W2065431624 cites W2040187234 @default.
• W2065431624 cites W2046061379 @default.
• W2065431624 cites W2046696671 @default.
• W2065431624 cites W2055581912 @default.
• W2065431624 cites W2058040756 @default.
• W2065431624 cites W2059105573 @default.
• W2065431624 cites W2061887764 @default.
• W2065431624 cites W2067254288 @default.
• W2065431624 cites W2072972888 @default.
• W2065431624 cites W2084763593 @default.
• W2065431624 cites W2088022602 @default.
• W2065431624 cites W2117514600 @default.
• W2065431624 cites W2133622062 @default.
• W2065431624 cites W2134376485 @default.
• W2065431624 cites W2139337055 @default.
• W2065431624 cites W2158729487 @default.
• W2065431624 cites W2167432245 @default.
• W2065431624 cites W2169144574 @default.
• W2065431624 cites W3094608223 @default.
• W2065431624 cites W4234475175 @default.
• W2065431624 cites W74561736 @default.
• W2065431624 doi "https://doi.org/10.1080/07391102.1996.10508887" @default.
• W2065431624 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8723769" @default.
• W2065431624 hasPublicationYear "1996" @default.
• W2065431624 type Work @default.
• W2065431624 sameAs 2065431624 @default.
• W2065431624 citedByCount "32" @default.
• W2065431624 countsByYear W20654316242013 @default.
• W2065431624 countsByYear W20654316242014 @default.
• W2065431624 countsByYear W20654316242015 @default.
• W2065431624 countsByYear W20654316242016 @default.
• W2065431624 countsByYear W20654316242017 @default.
• W2065431624 countsByYear W20654316242019 @default.
• W2065431624 countsByYear W20654316242021 @default.
• W2065431624 countsByYear W20654316242023 @default.
• W2065431624 crossrefType "journal-article" @default.
• W2065431624 hasAuthorship W2065431624A5026933296 @default.
• W2065431624 hasAuthorship W2065431624A5045061541 @default.
• W2065431624 hasAuthorship W2065431624A5064890753 @default.
• W2065431624 hasAuthorship W2065431624A5068337005 @default.
• W2065431624 hasConcept C115624301 @default.
• W2065431624 hasConcept C128765274 @default.
• W2065431624 hasConcept C170751736 @default.
• W2065431624 hasConcept C178790620 @default.
• W2065431624 hasConcept C181199279 @default.
• W2065431624 hasConcept C185592680 @default.
• W2065431624 hasConcept C18903297 @default.
• W2065431624 hasConcept C203036418 @default.
• W2065431624 hasConcept C2777289219 @default.
• W2065431624 hasConcept C2780912031 @default.
• W2065431624 hasConcept C2909420578 @default.
• W2065431624 hasConcept C41183919 @default.
• W2065431624 hasConcept C515207424 @default.
• W2065431624 hasConcept C55493867 @default.
• W2065431624 hasConcept C71240020 @default.
• W2065431624 hasConcept C8010536 @default.
• W2065431624 hasConcept C86803240 @default.
• W2065431624 hasConceptScore W2065431624C115624301 @default.
• W2065431624 hasConceptScore W2065431624C128765274 @default.
• W2065431624 hasConceptScore W2065431624C170751736 @default.
• W2065431624 hasConceptScore W2065431624C178790620 @default.
• W2065431624 hasConceptScore W2065431624C181199279 @default.
• W2065431624 hasConceptScore W2065431624C185592680 @default.
• W2065431624 hasConceptScore W2065431624C18903297 @default.
• W2065431624 hasConceptScore W2065431624C203036418 @default.

• next