EC Number | Application | Comment | Organism |
---|---|---|---|
2.7.1.175 | synthesis | enzymatic synthesis of maltose 1-phosphate | Mycolicibacterium smegmatis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.99.16 | 1,4-dideoxy-1,4-imino-D-arabinitol | - |
Mycolicibacterium smegmatis | |
2.4.99.16 | arsenate | - |
Mycolicibacterium smegmatis | |
2.4.99.16 | ATP | strong inhibition | Mycolicibacterium smegmatis | |
2.4.99.16 | D-glucose 1-phosphate | slight inhibition | Mycolicibacterium smegmatis | |
2.4.99.16 | D-glucose 6-phosphate | slight inhibition | Mycolicibacterium smegmatis | |
2.4.99.16 | diphosphate | slight inhibition | Mycolicibacterium smegmatis | |
2.4.99.16 | maltosaccharides | compete with glycogen for the transferred maltose | Mycolicibacterium smegmatis | |
2.4.99.16 | additional information | no inhibition by isofagomine or acarbose | Mycolicibacterium smegmatis | |
2.4.99.16 | phosphate | - |
Mycolicibacterium smegmatis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.99.16 | additional information | - |
additional information | kinetics, overview | Mycolicibacterium smegmatis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.175 | Mg2+ | required | Mycolicibacterium smegmatis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | Mycolicibacterium smegmatis | - |
phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | Mycolicibacterium smegmatis ATCC 14468 | - |
phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.99.16 | Mycolicibacterium smegmatis | Q9RP48 | - |
- |
2.4.99.16 | Mycolicibacterium smegmatis ATCC 14468 | Q9RP48 | - |
- |
2.7.1.175 | Mycolicibacterium smegmatis | - |
- |
- |
2.7.1.175 | Mycolicibacterium smegmatis ATCC 14468 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.4.99.16 | native enzyme GMPMT 89fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography and gel filtration | Mycolicibacterium smegmatis |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.4.99.16 | 0.76 | - |
purified enzyme, pH 7.0, 37°C | Mycolicibacterium smegmatis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | - |
Mycolicibacterium smegmatis | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose | Mycolicibacterium smegmatis | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
r | |
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | - |
Mycolicibacterium smegmatis ATCC 14468 | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
2.4.99.16 | alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose | Mycolicibacterium smegmatis ATCC 14468 | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
r | |
2.4.99.16 | additional information | GMPMT requires a high-molecular weight alpha-1,4-glucan as the acceptor. The enzyme can also transfer maltosyl units to maltosaccharides, e.g. maltotetraose to maltohexaose, overview | Mycolicibacterium smegmatis | ? | - |
? | |
2.4.99.16 | additional information | GMPMT requires a high-molecular weight alpha-1,4-glucan as the acceptor. The enzyme can also transfer maltosyl units to maltosaccharides, e.g. maltotetraose to maltohexaose, overview | Mycolicibacterium smegmatis ATCC 14468 | ? | - |
? | |
2.7.1.175 | ATP + maltose | - |
Mycolicibacterium smegmatis | ADP + maltose 1-phosphate | - |
? | |
2.7.1.175 | ATP + maltose | - |
Mycolicibacterium smegmatis ATCC 14468 | ADP + maltose 1-phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.99.16 | alpha1,4-glucan:maltose-1-P maltosyltransferase | - |
Mycolicibacterium smegmatis |
2.4.99.16 | GMPMT | - |
Mycolicibacterium smegmatis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.99.16 | 37 | - |
assay at | Mycolicibacterium smegmatis |
2.7.1.175 | 50 | - |
- |
Mycolicibacterium smegmatis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.99.16 | 7 | - |
assay at | Mycolicibacterium smegmatis |
2.7.1.175 | 8.2 | - |
- |
Mycolicibacterium smegmatis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.1.175 | ATP | dependent on | Mycolicibacterium smegmatis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.99.16 | metabolism | the enzyme catalyzes the last step in the conversion of trehalose to glycogen transfering maltose from maltose 1-phosphate to glycogen. Trehalose synthase, maltokinase, and GMPMT represent an additional pathway of glycogen synthesis using trehalose as the source of glucose | Mycolicibacterium smegmatis |
2.7.1.175 | metabolism | the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose | Mycolicibacterium smegmatis |