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Literature summary for 2.3.1.180 extracted from

  • Misra, N.; Patra, M.; Panda, P.; Sukla, L.; Mishra, B.
    Homology modeling and docking studies of FabH (beta-ketoacyl-ACP synthase III) enzyme involved in type II fatty acid biosynthesis of Chlorella variabilis: a potential algal feedstock for biofuel production (2013), J. Biomol. Struct. Dyn., 31, 241-257.
    View publication on PubMed

Application

Application Comment Organism
biofuel production the enzyme is interesting in order to develop engineered high oil-yielding microalgal strains for biofuel production Chlorella variabilis

Organism

Organism UniProt Comment Textmining
Chlorella variabilis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structural and dynamical aspect of catalytic mechanism of FabH, overview Chlorella variabilis ?
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Synonyms

Synonyms Comment Organism
beta-ketoacyl-ACP synthase III
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Chlorella variabilis
FabH
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Chlorella variabilis
KAS III
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Chlorella variabilis

General Information

General Information Comment Organism
additional information three-dimensional structure analysis, homology modeling and docking studies of beta-ketoacyl-ACP synthase III, FabH, enzyme involved in type II fatty acid biosynthesis of Chlorella variabilis, protein-protein docking and molecular dynamics simulation protocols. The FabH-ACP complex has the lowest docking energy score and shows the binding of ACP to the electropositive FabH surface with strong hydrogen bond interactions. The substrate-complexed FabH adopts a more stable conformation than the free enzyme. The FabH structure retains its stability throughout the simulation although noticeable displacements are observed in the loop regions. Molecular simulation studies suggest the importance of crucial hydrogen bonding of the conserved Arg91 of FabH with Glu53 and Asp56 of ACP for exhibiting high affinity between the enzyme and substrate Chlorella variabilis
physiological function beta-ketoacyl-acyl carrier protein synthase is a condensing enzyme catalyzing the initial elongation step of type II fatty acid biosynthetic process and acyl carrier protein (ACP) facilitates the shuttling of the fatty acyl intermediates to the active site of the respective enzymes in the pathway Chlorella variabilis