Sine Larsen
University of Copenhagen
287 Papers
2.1K Citations
Sine Larsen is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Crystal structure & Chemistry. The author has an hindex of 38, co-authored 287 publications. Previous affiliations of Sine Larsen include European Synchrotron Radiation Facility & European Bioinformatics Institute.
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Papers
Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31
Heidi A. Ernst,Leila Lo Leggio,Martin Willemoës,Gordon A. Leonard,Paul H. Blum,Sine Larsen,Sine Larsen +6 more
TL;DR: Structural comparisons with other GH families suggest that the GH31 enzymes belong to clan GH-D, including alpha-glucosidases from higher organisms, involved in glycogen degradation and glycoprotein processing.
Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase.
TL;DR: A resolution structure of ODCase complexed with the inhibitor 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid shows a closely packed dimer composed of two alpha/beta-barrels with two shared active sites, and the orientation of the orotate moiety of the substrate is unambiguously deduced.
Short strong hydrogen bonds in proteins: a case study of rhamnogalacturonan acetylesterase.
Annette Eva Langkilde,Søren M. Kristensen,Leila Lo Leggio,Anne Mølgaard,Jan H. Jensen,Jan H. Jensen,Andrew R. Houk,Jens-Christian N. Poulsen,Sakari Kauppinen,Sine Larsen,Sine Larsen +10 more
TL;DR: The short hydrogen bonds in rhamnogalacturonan acetylesterase have been investigated by structure determination of an active-site mutant, 1H NMR spectra and computational methods and comparisons are made to database statistics.
Active Site of Dihydroorotate Dehydrogenase A from Lactococcus lactis Investigated by Chemical Modification and Mutagenesis
TL;DR: The possible acid-base chemistry of Cys 130 is compared to previous work on mammalian dihydropyrimidine dehydrogenases, flavoenzymes, which catalyze the reversed reaction, namely the reduction of pyrimidine bases.