EC Tree |
2. Transferases |
2.4 Glycosyltransferases |
2.4.99 Transferring other glycosyl groups |
ID: | 2.4.99.16 |
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Description: | Starch synthase (maltosyl-transferring). |
Alternative Name: |
GMPMT. Alpha-1,4-glucan:maltose-1-P maltosyltransferase. |
Cath: | 3.20.20.80; 1.20.58.280; 2.60.40.10; 2.60.40.1180; |
Click one PDB to see exact 3D structure provided by NGL.
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 2.4.99.16 |
BRENDA Enzyme Link: | BRENDA 2.4.99.16 |
KEGG Enzyme Link: | KEGG2.4.99.16 |
BioCyc Enzyme Link: | BioCyc 2.4.99.16 |
ExPASy Enzyme Link: | ExPASy2.4.99.16 |
EC2PDB Enzyme Link: | EC2PDB 2.4.99.16 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.99.16 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.99.16 |
IntEnz Enzyme Link: | IntEnz 2.4.99.16 |
MEDLINE Enzyme Link: | MEDLINE 2.4.99.16 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:42692 | [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate |
RULE(radius=1) | |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. | Syson K, Stevenson CE, Rejzek M, Fairhurst SA, Nair A, Bruton CJ, Field RA, Chater KF, Lawson DM, Bornemann S | 2011 Nov 4 | 21914799 |
Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen. | Elbein AD, Pastuszak I, Tackett AJ, Wilson T, Pan YT | 2010 Mar 26 | 20118231 |