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Literature summary for 2.4.1.25 extracted from

  • Imamura, H.; Fushinobu, S.; Jeon, B.S.; Wakagi, T.; Matsuzawa, H.
    Identification of the catalytic residue of Thermococcus litoralis 4-alpha-glucanotransferase through mechanism-based labeling (2001), Biochemistry, 40, 12400-12406.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
genes of wild-type and mutant enzymes are coexpressed in Escherichia coli cells with GroELS, tRNA(AGA), and tRNA(AGG) Thermococcus litoralis

Protein Variants

Protein Variants Comment Organism
E123Q the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme Thermococcus litoralis
E129Q the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme Thermococcus litoralis

Organism

Organism UniProt Comment Textmining
Thermococcus litoralis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermococcus litoralis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chloro-4-nitrophenyl 4'''',6''''-O-(3-oxobutylidene)maltopentaoside + D-glucose the disproportionation reaction of the enzyme involves a ping-pong bi-bi mechanism. On the basis of this reaction mechanism, the glycosyl-enzyme intermediate, in which a donor substrate is covalently bound to the catalytic nucleophile, is trapped by treating the enzyme with 3-ketobutylidene-beta-2-chloro-4-nitrophenyl maltopentaoside in the absence of an acceptor and is detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry after peptic digestion Thermococcus litoralis ?
-
?
maltotriose + maltotriose
-
Thermococcus litoralis ?
-
?

Synonyms

Synonyms Comment Organism
TLGT
-
Thermococcus litoralis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
assay at Thermococcus litoralis