EC |
2.4.1.230 |
Accepted name: |
kojibiose phosphorylase |
Reaction: |
2-α-D-glucosyl-D-glucose + phosphate = D-glucose + β-D-glucose 1-phosphate |
Systematic name: |
2-α-D-glucosyl-D-glucose:phosphate β-D-glucosyltransferase |
Comments: |
The enzyme from Thermoanaerobacter brockii can act with α-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. The enzyme is inactive when dissaccharides with linkages other than α-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 206566-36-1 |
References: |
1. |
Chaen, H., Yamamoto, T., Nishimoto, T., Nakada, T., Fukuda, S., Sugimoto, T., Kurimoto, M. and Tsujisaka, Y. Purification and characterization of a novel phosphorylase, kojibiose phosphorylase, from Thermoanaerobium brockii. J. Appl. Glycosci. 46 (1999) 423–429. |
2. |
Chaen, H., Nishimoto, T., Nakada, T., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Enzymatic synthesis of kojioligosaccharides using kojibiose phosphorylase. J. Biosci. Bioeng. 92 (2001) 177–182. [DOI] [PMID: 16233080] |
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[EC 2.4.1.230 created 2003] |
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EC |
2.4.1.333 |
Accepted name: |
1,2-β-oligoglucan phosphorylase |
Reaction: |
[(1→2)-β-D-glucosyl]n + phosphate = [(1→2)-β-D-glucosyl]n-1 + α-D-glucose 1-phosphate |
Systematic name: |
1,2-β-D-glucan:phosphate α-D-glucosyltransferase |
Comments: |
The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9:e92353 (2014). [DOI] [PMID: 24647662] |
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[EC 2.4.1.333 created 2014] |
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EC |
2.4.1.391 |
Accepted name: |
β-1,2-glucosyltransferase |
Reaction: |
[(1→2)-β-D-glucosyl]n + a D-glucoside = [(1→2)-β-D-glucosyl]n-1 + a β-D-glucosyl-(1→2)-D-glucoside |
Systematic name: |
1,2-β-D-glucan:D-glucoside 2-β-D-glucosyltransferase (configuration-retaining) |
Comments: |
The enzyme, characterized from the bacterium Ignavibacterium album, transfers a glucosyl residue from the non-reducing end of a 1,2-β-D-glucan to a glucose residue of an acceptor molecule, forming a β(1,2) linkage. The donor molecule can be as small as sophorose (which contains two glucosyl residues). The enzyme has a very broad specificity for the acceptor, and can act on various aryl- and alkyl-glucosides. In addition, the accepting glucose unit can be in either α or β configuration. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kobayashi, K., Shimizu, H., Tanaka, N., Kuramochi, K., Nakai, H., Nakajima, M. and Taguchi, H. Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J. Biol. Chem. 298:101606 (2022). [DOI] [PMID: 35065074] |
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[EC 2.4.1.391 created 2022] |
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EC |
3.2.1.214 |
Accepted name: |
exo β-1,2-glucooligosaccharide sophorohydrolase (non-reducing end) |
Reaction: |
[(1→2)-β-D-glucosyl]n + H2O = sophorose + [(1→2)-β-D-glucosyl]n-2 |
Glossary: |
sophorose = β-D-glucopyranosyl-(1→2)-D-glucopyranose |
Systematic name: |
exo (1→2)-β-D-glucooligosaccharide sophorohydrolase (non-reducing end) |
Comments: |
The enzyme, characterized from the bacterium Parabacteroides distasonis, specifically hydrolyses (1→2)-β-D-glucooligosaccharides to sophorose. The best substrates are the tetra- and pentasaccharides. The enzyme is not able to cleave the trisaccharide, and activity with longer linear (1→2)-β-D-glucans is quite low. This enzyme acts in exo mode and is not able to hydrolyse cyclic (1→2)-β-D-glucans. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Shimizu, H., Nakajima, M., Miyanaga, A., Takahashi, Y., Tanaka, N., Kobayashi, K., Sugimoto, N., Nakai, H. and Taguchi, H. Characterization and structural analysis of a novel exo-type enzyme acting on β-1,2-glucooligosaccharides from Parabacteroides distasonis. Biochemistry 57 (2018) 3849–3860. [PMID: 29763309] |
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[EC 3.2.1.214 created 2020] |
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