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Literature summary for 1.4.1.27 extracted from

  • Lokanath, N.; Kuroishi, C.; Okazaki, N.; Kunishima, N.
    Crystal structure of a component of glycine cleavage system T-protein from Pyrococcus horikoshii OT3 at 1.5 A resolution (2005), Proteins, 58, 769-773 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of component T-protein, at 1.5 A resolution. The dimeric state might be essential for the function. The role of residue Glu100 might be the activation of the N10 atom of tetrahodrofolate by increasing its nucleophilic character. The H-protein-T-protein interface includes invariant residues Arg327, Tyr330, and Arg376 of domain III, and Lys20, Phe24, Gly26, Ser35, Ile36, Leu248, Gly249, Asp252, Thr253, Arg255, and Leu262 of domains I and II Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58888 i.e. aminomethyltransferase component T-protein, cf. EC 2.1.2.10
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Synonyms

Synonyms Comment Organism
GCVT
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Pyrococcus horikoshii
T-protein
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Pyrococcus horikoshii