Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction.
Gräwert
Tobias
T
Center for Integrated Protein Science, Lehrstuhl für Biochemie, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany. tobias.graewert@ch.tum.de
Rohdich
Felix
F
Span
Ingrid
I
Bacher
Adelbert
A
Eisenreich
Wolfgang
W
Eppinger
Jörg
J
Groll
Michael
M
D055162:Biocatalysis; D020134:Catalytic Domain; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D045782:Hemiterpenes / Q000096:biosynthesis / Q000737:chemistry; D009943:Organophosphorus Compounds / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D029968:Escherichia coli Proteins; D045782:Hemiterpenes; D009943:Organophosphorus Compounds; D011994:Recombinant Proteins; C004809:isopentenyl pyrophosphate; C043060:3,3-dimethylallyl pyrophosphate; D010088:Oxidoreductases; C109866:ispH protein, E coli