Crystallization (Comment) | Organism |
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comparative docking analysis shows that enzyme-substrate complex is forming similar Schiff base intermediate and conducts C3-C4 bond cleavage by forming hydrogen bonding with reaction catalyzing Glu191, reactive Lys150, and Schiff base forming Lys233. The noncovalent complex with inhibitor mannitol-1, 6 bisphosphate is forming cabinolamine precursor and the proton transfer by the formation of hydrogen bond between mannitol-1, 6 bisphosphate O2 with Glu191 enabling stabilization of cabinolamine transition state, which confirms the similar inhibition mechanism | Heterodera glycines |
Organism | UniProt | Comment | Textmining |
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Heterodera glycines | Q9GPK1 | - |
- |