Enzymes
| UniProtKB help_outline | 327 proteins |
| Enzyme classes help_outline |
|
| GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline α-maltose Identifier CHEBI:18167 (Beilstein: 1292753; CAS: 4482-75-1) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline GUBGYTABKSRVRQ-ASMJPISFSA-N SMILEShelp_outline OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-maltose Identifier CHEBI:18147 (Beilstein: 90844,5758727; CAS: 133-99-3,69-79-4) help_outline Charge 0 Formula C12H22O11 InChIKeyhelp_outline GUBGYTABKSRVRQ-QUYVBRFLSA-N SMILEShelp_outline OC[C@H]1O[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@H](O)[C@H]2O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21228 | RHEA:21229 | RHEA:21230 | RHEA:21231 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
A novel enzyme, maltose 1-epimerase from Lactobacillus brevis IFO 3345.
Shirokane Y., Suzuki M.
A novel enzyme, maltose 1-epimerase (MER), that catalyzes the interconversion of alpha and beta anomers of maltose was found in a cell-free extract of Lactobacillus brevis IFO 3345, and MER was purified to homogeneity from the crude extract. The M(r) of the enzyme was estimated to be 43,000 and 45 ... >> More
A novel enzyme, maltose 1-epimerase (MER), that catalyzes the interconversion of alpha and beta anomers of maltose was found in a cell-free extract of Lactobacillus brevis IFO 3345, and MER was purified to homogeneity from the crude extract. The M(r) of the enzyme was estimated to be 43,000 and 45,000 by HPLC gel filtration and SDS-PAGE, respectively. It showed optimum activity at pH 6.5-7.0. This novel enzyme catalyzed the conversion of beta-maltose more effectively than disaccharides such as alpha-lactose and beta-cellobiose, whereas the relative velocities for beta- and alpha-D-glucose were about one forth of that for beta-maltose. << Less