Enzymes
UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
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Name help_outline
(1→2)-β-D-mannan
Identifier
CHEBI:59573
Charge
0
Formula
(C6H10O5)n.H2O
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:12390Polymer name: [(1→2)-β-D-mannosyl](n)Polymerization index help_outline nFormula H2O(C6H10O5)nCharge (0)(0)nMol File for the polymer
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Identifier: RHEA-COMP:12391Polymer name: [(1→2)-β-D-mannosyl](n-1)Polymerization index help_outline n-1Formula H2O(C6H10O5)n-1Charge (0)(0)n-1Mol File for the polymer
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- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-mannose 1-phosphate Identifier CHEBI:58409 (Beilstein: 3911528) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline HXXFSFRBOHSIMQ-RWOPYEJCSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:49408 | RHEA:49409 | RHEA:49410 | RHEA:49411 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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MetaCyc help_outline |
Publications
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Discovery of two beta-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514.
Chiku K., Nihira T., Suzuki E., Nishimoto M., Kitaoka M., Ohtsubo K., Nakai H.
We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors, respectively, in the presence of the donor α ... >> More
We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors, respectively, in the presence of the donor α-d-mannose 1-phosphate. Kinetic analysis of the phosphorolytic reaction toward 1,2-β-oligomannan revealed that these enzymes followed a typical sequential Bi Bi mechanism. The kinetic parameters of the phosphorolysis of 1,2-β-oligomannan indicate that Teth514_1788 and Teth514_1789 prefer 1,2-β-oligomannans containing a DP ≥3 and β-1,2-Man2, respectively. These results indicate that the two enzymes are novel inverting phosphorylases that exhibit distinct chain-length specificities toward 1,2-β-oligomannan. Here, we propose 1,2-β-oligomannan:phosphate α-d-mannosyltransferase as the systematic name and 1,2-β-oligomannan phosphorylase as the short name for Teth514_1788 and β-1,2-mannobiose:phosphate α-d-mannosyltransferase as the systematic name and β-1,2-mannobiose phosphorylase as the short name for Teth514_1789. << Less
PLoS ONE 9:e114882-e114882(2014) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.