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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003595naa a2200397 4500
001oai:DiVA.org:umu-187197
003SwePub
008210908s2021 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1871972 URI
0247 a https://doi.org/10.1021/acs.biochem.1c002212 DOI
040 a (SwePub)umu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Ojeda-May, Pedrou Umeå universitet,Kemiska institutionen,Högpresterande beräkningscentrum norr (HPC2N)4 aut0 (Swepub:umu)peoj0002
2451 0a Dynamic Connection between Enzymatic Catalysis and Collective Protein Motions
264 c 2021-07-12
264 1b American Chemical Society (ACS),c 2021
338 a print2 rdacarrier
520 a Enzymes employ a wide range of protein motions to achieve efficient catalysis of chemical reactions. While the role of collective protein motions in substrate binding, product release, and regulation of enzymatic activity is generally understood, their roles in catalytic steps per se remain uncertain. Here, molecular dynamics simulations, enzyme kinetics, X-ray crystallography, and nuclear magnetic resonance spectroscopy are combined to elucidate the catalytic mechanism of adenylate kinase and to delineate the roles of catalytic residues in catalysis and the conformational change in the enzyme. This study reveals that the motions in the active site, which occur on a time scale of picoseconds to nanoseconds, link the catalytic reaction to the slow conformational dynamics of the enzyme by modulating the free energy landscapes of subdomain motions. In particular, substantial conformational rearrangement occurs in the active site following the catalytic reaction. This rearrangement not only affects the reaction barrier but also promotes a more open conformation of the enzyme after the reaction, which then results in an accelerated opening of the enzyme compared to that of the reactant state. The results illustrate a linkage between enzymatic catalysis and collective protein motions, whereby the disparate time scales between the two processes are bridged by a cascade of intermediate-scale motion of catalytic residues modulating the free energy landscapes of the catalytic and conformational change processes.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Ul Mushtaq, Ameequ Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)amul0005
7001 a Rogne, Peru Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)pero0018
7001 a Verma, Apoorvu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)apve0002
7001 a Ovchinnikov, Victor4 aut
7001 a Grundström, Christinu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)chgr0001
7001 a Dulko-Smith, Beata4 aut
7001 a Sauer, Uwe H.u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)uwsa0001
7001 a Wolf-Watz, Magnus,d 1971-u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)maswoz04
7001 a Nam, Kwangho4 aut
7102 a Umeå universitetb Kemiska institutionen4 org
7730 t Biochemistryd : American Chemical Society (ACS)g 60:28, s. 2246-2258q 60:28<2246-2258x 0006-2960x 1520-4995
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-187197
8564 8u https://doi.org/10.1021/acs.biochem.1c00221

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