KEGG   ENZYME: 2.4.1.394
Entry
EC 2.4.1.394                Enzyme                                 
Name
4,6-alpha-glucanotransferase (linear substrates/linear products);
gtfB (gene name) (ambiguous);
gtfC (gene name)
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
linear (1->4)-alpha-D-glucan:(1->4)/(1->6)-alpha-D-glucan 6-alpha-D-glucosyltransferase
Reaction(IUBMB)
formation of a linear isomalto/malto-polysaccharide from linear malto-oligosaccharides
Comment
The enzyme, originally discovered in lactic acid bacteria but later found in other organisms, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving alpha(1->4) linkages from the non-reducing end of linear maltooligosaccharides and synthesizing linear alpha(1->6)-glucan chains. It also possesses an endo-alpha(1->4)-glycosidase activity. Due to its narrow binding groove, it is not able to act on branched substrates. cf. EC 2.4.1.396, 4,6-alpha-glucanotransferase (linear and branched substrates, branched products).
History
EC 2.4.1.394 created 2023
Orthology
K27184  4,6-alpha-glucanotransferase (linear substrates/linear products)
Genes
GEAGARCT_00912(gtfC)
BCKBCO26_0382
BCOABF29_2884
ESIExig_2648
EANEab7_2453
EXUESP131_00130
EACEKKI46_14365
Reference
1  [PMID:15528655]
  Authors
Kralj S, van Geel-Schutten GH, Dondorff MMG, Kirsanovs S, van der Maarel MJEC, Dijkhuizen L.
  Title
Glucan synthesis in the genus Lactobacillus: isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains.
  Journal
Microbiology (Reading) 150:3681-3690 (2004)
DOI:10.1099/mic.0.27321-0
  Sequence
Reference
2  [PMID:21948833]
  Authors
Kralj S, Grijpstra P, van Leeuwen SS, Leemhuis H, Dobruchowska JM, van der Kaaij RM, Malik A, Oetari A, Kamerling JP, Dijkhuizen L.
  Title
4,6-alpha-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70.
  Journal
Appl Environ Microbiol 77:8154-63 (2011)
DOI:10.1128/AEM.05735-11
  Sequence
Reference
3  [PMID:22138321]
  Authors
Dobruchowska JM, Gerwig GJ, Kralj S, Grijpstra P, Leemhuis H, Dijkhuizen L, Kamerling JP.
  Title
Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-alpha-glucanotransferase enzyme from Lactobacillus reuteri 121.
  Journal
Glycobiology 22:517-28 (2012)
DOI:10.1093/glycob/cwr167
Reference
4  [PMID:22361861]
  Authors
Leemhuis H, Dijkman WP, Dobruchowska JM, Pijning T, Grijpstra P, Kralj S, Kamerling JP, Dijkhuizen L.
  Title
4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily.
  Journal
Appl Microbiol Biotechnol 97:181-93 (2013)
DOI:10.1007/s00253-012-3943-1
Reference
5  [PMID:26590275]
  Authors
Gangoiti J, Pijning T, Dijkhuizen L.
  Title
The Exiguobacterium sibiricum 255-15 GtfC Enzyme Represents a Novel Glycoside Hydrolase 70 Subfamily of 4,6-alpha-Glucanotransferase Enzymes.
  Journal
Appl Environ Microbiol 82:756-66 (2016)
DOI:10.1128/AEM.03420-15
  Sequence
[esi:Exig_2648]
Reference
6  [PMID:28065507]
  Authors
Bai Y, Gangoiti J, Dijkstra BW, Dijkhuizen L, Pijning T.
  Title
Crystal Structure of 4,6-alpha-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from alpha-Amylases in Oral Bacteria.
  Journal
Structure 25:231-242 (2017)
DOI:10.1016/j.str.2016.11.023
  Sequence
Reference
7  [PMID:34427087]
  Authors
Te Poele EM, van der Hoek SE, Chatziioannou AC, Gerwig GJ, Duisterwinkel WJ, Oudhuis LAACM, Gangoiti J, Dijkhuizen L, Leemhuis H.
  Title
GtfC Enzyme of Geobacillus sp. 12AMOR1 Represents a Novel Thermostable Type of GH70 4,6-alpha-Glucanotransferase That Synthesizes a Linear Alternating (alpha1 --> 6)/(alpha1 --> 4) alpha-Glucan and Delays Bread Staling.
  Journal
J Agric Food Chem 69:9859-9868 (2021)
DOI:10.1021/acs.jafc.1c03475
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.394
IUBMB Enzyme Nomenclature: 2.4.1.394
ExPASy - ENZYME nomenclature database: 2.4.1.394
BRENDA, the Enzyme Database: 2.4.1.394
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