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Literature summary for 4.1.2.13 extracted from

  • Prasad, C.S.; Gupta, S.; Kumar, H.; Tiwari, M.
    Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes (2013), Bioinformation, 9, 1-8.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Heterodera glycines Q9GPK1
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