Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.B34 extracted from

  • Bai, Y.; Gangoiti, J.; Dijkstra, B.W.; Dijkhuizen, L.; Pijning, T.
    Crystal structure of 4,6-alpha-glucanotransferase supports diet-driven evolution of GH70 enzymes from alpha-amylases in oral bacteria (2017), Structure, 25, 231-242 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene gtfB, genomic mapping and phylogenetic analysis, recombinant expression of wild-type and truncated mutant enzymes Limosilactobacillus reuteri

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type enzyme in apoform and in complex with maltohexaose, and enzyme mutant D1015N in complex with maltopentaose, crystallized by the hanging-drop vapor diffusion method and a microseeding protocol, X-ray diffraction structre determination and analysis at 1.80-2.19 A resolution, molecular replacement using domains A, B, C, and IV of the crystal structure of Lactobacillus reuteri 180 GTF180-DELTAN (PDB ID 3KLK) as a search model Limosilactobacillus reuteri

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion GtfB-DELTANDELTAV mutant D1015N Limosilactobacillus reuteri

Organism

Organism UniProt Comment Textmining
Limosilactobacillus reuteri A0A0U5F702
-
-
Limosilactobacillus reuteri 121 A0A0U5F702
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview Limosilactobacillus reuteri ?
-
-
additional information malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview Limosilactobacillus reuteri 121 ?
-
-

Synonyms

Synonyms Comment Organism
GtfB
-
Limosilactobacillus reuteri
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein UniProt Limosilactobacillus reuteri

General Information

General Information Comment Organism
evolution the crystal structure analysis of 4,6-alpha-glucanotransferase supports diet-driven evolution of GH70 enzymes from alpha-amylases in oral bacteria, overview. Mode of action and detailing the structural changes accompanying the proposed evolution of glycoside hydrolase family 70 (GH70). The enzyme belongs to the glycoside hydrolase family 70 (GH70) Limosilactobacillus reuteri
additional information structure-function analysis, modeling and docking, overview. Mechanism and mode of action of GtfB in comparison with alpha-amylase and glucansucrase Limosilactobacillus reuteri