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Sökning: WFRF:(Brandsdal Bjørn O.) > Structure and Mecha...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003987naa a2200409 4500
001oai:DiVA.org:uu-476617
003SwePub
008220621s2022 | |||||||||||000 ||eng|
024a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4766172 URI
024a https://doi.org/10.1021/acs.biochem.2c000872 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a van der Ent, Florianu Uppsala universitet,Beräkningsbiologi och bioinformatik4 aut0 (Swepub:uu)flova102
2451 0a Structure and Mechanism of a Cold-Adapted Bacterial Lipase
264 c 2022-05-03
264 1b American Chemical Society (ACS),c 2022
338 a electronic2 rdacarrier
520 a The structural origin of enzyme cold-adaptation has been the subject of considerable research efforts in recent years. Comparative studies of orthologous mesophilic-psychrophilic enzyme pairs found in nature are an obvious strategy for solving this problem, but they often suffer from relatively low sequence identity of the enzyme pairs. Small bacterial lipases adapted to distinctly different temperatures appear to provide an excellent model system for these types of studies, as they may show a very high degree of sequence conservation. Here, we report the first crystal structures of lipase A from the psychrophilic bacterium Bacillus pumilus, which confirm the high structural similarity to the mesophilic Bacillus subtilis enzyme, as indicated by their 81% sequence identity. We further employ extensive QM/MM calculations to delineate the catalytic reaction path and its energetics. The computational prediction of a rate-limiting deacylation step of the enzymatic ester hydrolysis reaction is verified by stopped-flow experiments, and steady-state kinetics confirms the psychrophilic nature of the B. pumilus enzyme. These results provide a useful benchmark for examining the structural basis of cold-adaptation and should now make it possible to disentangle the effects of the 34 mutations between the two enzymes on catalytic properties and thermal stability.
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
700a Lund, Bjarte A.u Uppsala universitet,Institutionen för cell- och molekylärbiologi,Arctic Univ Norway, Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.4 aut
700a Svalberg, Linnu Uppsala universitet,Institutionen för cell- och molekylärbiologi4 aut0 (Swepub:uu)linsv807
700a Purg, Mihau Uppsala universitet,Institutionen för cell- och molekylärbiologi4 aut0 (Swepub:uu)mihpu392
700a Chukwu, Ghisleanu Uppsala universitet,Biokemi4 aut0 (Swepub:uu)ghich737
700a Widersten, Mikaelu Uppsala universitet,Biokemi4 aut0 (Swepub:uu)mikawide
700a V. Isaksen, Geiru Arctic Univ Norway, Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.4 aut
700a Brandsdal, Bjørn O.u Arctic Univ Norway, Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.4 aut
700a Åqvist, Johanu Uppsala universitet,Beräkningsbiologi och bioinformatik,Arctic Univ Norway, Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.4 aut0 (Swepub:uu)johanaq
710a Uppsala universitetb Beräkningsbiologi och bioinformatik4 org
773t Biochemistryd : American Chemical Society (ACS)g 61:10, s. 933-942q 61:10<933-942x 0006-2960x 1520-4995
856u https://doi.org/10.1021/acs.biochem.2c00087y Fulltext
856u https://uu.diva-portal.org/smash/get/diva2:1673545/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-476617
8564 8u https://doi.org/10.1021/acs.biochem.2c00087

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