Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Ingo Korndörfer"'
Autor:
Thomas Dams, Rainer Jaenicke, Ralf Ostendorp, Günter Auerbach, Ingo Korndörfer, Lars Prade, Robert Huber
Publikováno v:
Structure. 6(6):769-781
Background: L(+)-Lactate dehydrogenase (LDH) catalyzes the last step in anaerobic glycolysis, the conversion of pyruvate to lactate, with the concomitant oxidation of NADH. Extensive physicochemical and structural investigations of LDHs from both mes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1041800c876a6521aed51701bf98b073
Publikováno v:
Journal of Molecular Biology. 246:227-239
The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1369ad3d95ba2d7b6ee9e7a97126e35
https://doi.org/10.1006/jmbi.1994.0078
https://doi.org/10.1006/jmbi.1994.0078
Publikováno v:
Journal of molecular biology. 246(4)
The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophile Thermotoga maritima was determined by Patterson search methods using the known structure of the Bacillus stearothermophilus enzyme. The structure was ref
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d05813a99138448de4ba681ace1a63bc
https://pubmed.ncbi.nlm.nih.gov/7877172
https://pubmed.ncbi.nlm.nih.gov/7877172