| Maltose α-D-glucosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.16 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a maltose α-D-glucosyltransferase (EC 5.4.99.16) is an enzyme that catalyzes the chemical reaction
- maltose alpha,alpha-trehalose
alpha,alpha-trehaloseHence, this enzyme has one substrate, maltose, and one product, alpha,alpha-trehalose.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is maltose alpha-D-glucosylmutase. Other names in common use include trehalose synthase, and maltose glucosylmutase. This enzyme participates in starch and sucrose metabolism.
References
- Sugimoto T, Kurimoto M, Tsujisaka Y (1995). "Existence of a novel enzyme converting maltose to trehalose". Biosci. Biotechnol. Biochem. 59 (11): 2189–2190. doi:10.1271/bbb.59.2189.
- Kurimoto M, Tsujisaka Y (1996). "Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48". Biosci. Biotechnol. Biochem. 60 (4): 640–4. doi:10.1271/bbb.60.640. PMID 8829531.
| Isomerase: mutases (EC 5.4) | |
|---|---|
| 5.4.1 Acyl Groups | |
| 5.4.2 Phosphomutases | |
| 5.4.99 Other groups | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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