ID: | 2.4.1.340 |
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Description: | 1,2-beta-oligomannan phosphorylase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.4.1.340 |
BRENDA Enzyme Link: | BRENDA 2.4.1.340 |
KEGG Enzyme Link: | KEGG2.4.1.340 |
BioCyc Enzyme Link: | BioCyc 2.4.1.340 |
ExPASy Enzyme Link: | ExPASy2.4.1.340 |
EC2PDB Enzyme Link: | EC2PDB 2.4.1.340 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.1.340 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.1.340 |
IntEnz Enzyme Link: | IntEnz 2.4.1.340 |
MEDLINE Enzyme Link: | MEDLINE 2.4.1.340 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:49408 | [(1->2)-beta-D-mannosyl](n) + phosphate = [(1->2)-beta-D-mannosyl](n-1) + alpha-D-mannose 1-phosphate |
RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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Discovery of two β-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 | 2014 | 25500577 |