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Literature summary for 2.4.1.18 extracted from

  • Chaen, K.; Noguchi, J.; Omori, T.; Kakuta, Y.; Kimura, M.
    Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose (2012), Biochem. Biophys. Res. Commun., 424, 508-511.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Oryza sativa

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant E399Q in complex with maltopentaose at a resolution of 2.2 A. Maltopentaose binds to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48, and alpha-amylase domain. In addition, glucose moieties can be observed at molecular surfaces on the N-terminal helix alpha2 and carbohydrate-binding module 48 Oryza sativa

Protein Variants

Protein Variants Comment Organism
E399Q supposed general acid/base residue, crystallization data Oryza sativa

Organism

Organism UniProt Comment Textmining
Oryza sativa Q01401 isoform branching enzyme I
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Synonyms

Synonyms Comment Organism
SBE1
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Oryza sativa