1.3.3.11: pyrroloquinoline-quinone synthase
This is an abbreviated version!
For detailed information about pyrroloquinoline-quinone synthase, go to the full flat file.
Word Map on EC 1.3.3.11
-
1.3.3.11
-
quinoproteins
-
methanol
-
prosthetic
-
dehydrogenases
-
radiodurans
-
extorquens
-
methylobacterium
-
pqq-containing
-
deinococcus
-
calcoaceticus
-
acinetobacter
-
synthesis
-
biotechnology
-
analysis
- 1.3.3.11
-
quinoproteins
- methanol
-
prosthetic
- dehydrogenases
- radiodurans
- extorquens
-
methylobacterium
-
pqq-containing
- deinococcus
- calcoaceticus
-
acinetobacter
- synthesis
- biotechnology
- analysis
Reaction
Synonyms
PqqC, PqqC/D, pyrroloquinoline quinone synthase C, pyrroloquinoline-quinone synthase, pyrroloquinoline/quinone synthesis protein C, quinoprotein dehydrogenase
ECTree
Advanced search results
Crystallization
Crystallization on EC 1.3.3.11 - pyrroloquinoline-quinone synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
purified recombinant enzyme mutants H154S/PQQ Y175F/PQQ Y175S/R179S in complex with intermediate 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid, sitting drop-vapor diffusion method, optimized conditions for each mutant: 0.1 M HEPES, pH 7.0, 0.5% w/v PEG 8000 for mutant H154S/PQQ complex, 0.2 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% w/v PEGl 3350 for mutant Y175F/PQQ complex, and 0.2 M sodium chloride, 0.1 M Tris, pH 8.5, 25% w/v PEG 3350 for mutant R179S/Y175S/intermediate complex, all at 20°C, X-ray diffraction structure determination and analysis at 1.3-2.35 A resolution