ID: | 2.4.1.139 |
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Description: | Maltose synthase. |
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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 2.4.1.139 |
BRENDA Enzyme Link: | BRENDA 2.4.1.139 |
KEGG Enzyme Link: | KEGG2.4.1.139 |
BioCyc Enzyme Link: | BioCyc 2.4.1.139 |
ExPASy Enzyme Link: | ExPASy2.4.1.139 |
EC2PDB Enzyme Link: | EC2PDB 2.4.1.139 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.1.139 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.1.139 |
IntEnz Enzyme Link: | IntEnz 2.4.1.139 |
MEDLINE Enzyme Link: | MEDLINE 2.4.1.139 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:22320 | 2 alpha-D-glucose 1-phosphate + H2O = maltose + 2 phosphate |
RULE(radius=1) | [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].([*:6]-[OH;+0:7].[*:8]=[P;H0;+0:9](-[*:10])(-[*:11])-[O;H0;+0:12]-[*:13]).[OH2;+0:14]>>([*:6]-[O;H0;+0:7]-[CH;+0:3](-[*:4])-[*:5].[*:13]-[OH;+0:12]).[*:1]-[OH;+0:2].[*:8]=[P;H0;+0:9](-[*:10])(-[*:11])-[OH;+0:14] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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Characterization of maltose biosynthesis from α-D-glucose-1-phosphate in Spinacia oleracea. L. | Schilling N | 1982 Mar | 24275923 |