| 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 |
2.4.1.279 |
| Accepted name: |
nigerose phosphorylase |
| Reaction: |
3-O-α-D-glucopyranosyl-D-glucopyranose + phosphate = D-glucose + β-D-glucose 1-phosphate |
| Glossary: |
3-O-α-D-glucopyranosyl-D-glucopyranose = nigerose |
| Other name(s): |
cphy1874 (gene name) |
| Systematic name: |
3-O-α-D-glucopyranosyl-D-glucopyranose:phosphate β-D-glucosyltransferase |
| Comments: |
The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230, kojibiose phosphorylase). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Nihira, T., Nakai, H., Chiku, K. and Kitaoka, M. Discovery of nigerose phosphorylase from Clostridium phytofermentans. Appl. Microbiol. Biotechnol. 93 (2012) 1513–1522. [DOI] [PMID: 21808968] |
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| [EC 2.4.1.279 created 2012] |
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| EC |
2.4.1.282 |
| Accepted name: |
3-O-α-D-glucosyl-L-rhamnose phosphorylase |
| Reaction: |
3-O-α-D-glucopyranosyl-L-rhamnopyranose + phosphate = L-rhamnopyranose + β-D-glucose 1-phosphate |
| Other name(s): |
cphy1019 (gene name) |
| Systematic name: |
3-O-α-D-glucopyranosyl-L-rhamnopyranose:phosphate β-D-glucosyltransferase |
| Comments: |
The enzyme does not phosphorylate α,α-trehalose, kojibiose, nigerose, or maltose. In the reverse phosphorolysis reaction the enzyme is specific for L-rhamnose as acceptor and β-D-glucose 1-phosphate as donor. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Nihira, T., Nakai, H. and Kitaoka, M. 3-O-α-D-glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans. Carbohydr. Res. 350 (2012) 94–97. [DOI] [PMID: 22277537] |
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| [EC 2.4.1.282 created 2012] |
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| EC |
3.2.1.115 |
| Accepted name: |
branched-dextran exo-1,2-α-glucosidase |
| Reaction: |
Hydrolysis of (1→2)-α-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose |
| Other name(s): |
dextran 1,2-α-glucosidase; dextran α-1,2-debranching enzyme; 1,2-α-D-glucosyl-branched-dextran 2-glucohydrolase |
| Systematic name: |
(1→2)-α-D-glucosyl-branched-dextran 2-glucohydrolase |
| Comments: |
Has a much lower activity with kojibiose and kojitriose. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72840-94-9 |
| References: |
| 1. |
Kobayashi, M., Mitsuishi, Y., and Matsuda, K. Pronounced hydrolysis of highly branched dextrans with a new type of dextranase. Biochem. Biophys. Res. Commun. 80(2) (1978) 306–312. [DOI] [PMID: 623663] |
| 2. |
Mitsuishi, Y., Kobayashi, M. and Matsuda, K. Dextran α-1,2-debranching enzyme from Flavobacterium sp. M-73: its production and purification. Agric. Biol. Chem. 43 (1979) 2283–2290. [DOI] |
| 3. |
Mitsuishi, Y., Kobayashi, M. and Matsuda, K. Dextran α-(1→2)-debranching enzyme from Flavobacterium sp. M-73. Properties and mode of action. Carbohydr. Res. 83 (1980) 303–313. [DOI] [PMID: 7407800] |
| 4. |
Miyazaki, T., Tanaka, H., Nakamura, S., Dohra, H. and Funane, K. Identification and characterization of dextran α-1,2-debranching enzyme from Microbacterium dextranolyticum. J. Appl. Glycosci. (1999) 70 (2023) 15–24. [DOI] [PMID: 37033117] |
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| [EC 3.2.1.115 created 1989, modified 2023] |
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| EC |
3.2.1.216 |
| Accepted name: |
kojibiose hydrolase |
| Reaction: |
kojibiose + H2O = β-D-glucopyranose + D-glucopyranose |
| Glossary: |
kojibiose = α-D-glucopyranosyl-(1→2)-D-glucopyranose |
| Other name(s): |
kojibiase |
| Systematic name: |
kojibiose glucohydrolase (configuration-inverting) |
| Comments: |
The enzyme, characterized from the bacteria Flavobacterium johnsoniae and Mucilaginibacter mallensis, uses anomer-inverting mechanism to release β-glucose from the non-reducing ends of kojibiose and α-1,2-oligoglucans with a higher degree of polymerization. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Nakamura, S., Nihira, T., Kurata, R., Nakai, H., Funane, K., Park, E.Y. and Miyazaki, T. Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. J. Biol. Chem. :101366 (2021). [DOI] [PMID: 34728215] |
| 2. |
De Beul, E., Jongbloet, A., Franceus, J. and Desmet, T. Discovery of a kojibiose hydrolase by analysis of specificity-determining correlated positions in glycoside hydrolase family 65. Molecules 26 (2021) 6321. [DOI] [PMID: 34684901] |
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| [EC 3.2.1.216 created 2022] |
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