EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.B8 | expression as malZ-yvdF fusion protein in Escherichia coli strain JT1 | Bacillus subtilis |
3.2.1.B8 | expression as malZ-yvdF fusion protein in Escherichia coli strain JT1 | Escherichia coli K-12 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.B8 | additional information | construction of a malZ-yvdF fusion enzyme, MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4. Construction of yvdF, amyX, and yvdF amyX mutant strains, amyX encodes the a debranching enzyme pullulanase. The yvdF mutant exhibits limited degradation of the substrates beta-cyclodextrin and maltoheptaose, oligosaccharides spectrum, overview | Bacillus subtilis |
3.2.1.B8 | additional information | construction of a malZ-yvdF fusion enzyme, substrate specificity, overview | Escherichia coli K-12 |
3.2.1.41 | additional information | construction of an amyX knockout strain and a glycogen overproducing glg strain with or without knockdown of amyX. The amyX glg strain accumulates significantly larger amounts of glycogen than the glg mutant, molecular masses of theglycogens, overview. Glycogen samples from the amyX glg strain exhibits average molecular masses two and three times larger, respectively, than that of glycogen from the glg mutant | Bacillus subtilis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.B8 | cytoplasm | YvdF is distributed on both sides of the cytoplasmic membrane and in the periplasm during vegetative growth but in the cytoplasm of prespores | Bacillus subtilis | 5737 | - |
3.2.1.B8 | periplasm | YvdF is distributed on both sides of the cytoplasmic membrane and in the periplasm during vegetative growth but in the cytoplasm of prespores | Bacillus subtilis | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.B8 | Bacillus subtilis | - |
gene yvdF | - |
3.2.1.B8 | Bacillus subtilis 168 | - |
gene yvdF | - |
3.2.1.B8 | Escherichia coli K-12 | - |
gene malZ | - |
3.2.1.41 | Bacillus subtilis | - |
gene amyX | - |
3.2.1.41 | Bacillus subtilis 168 | - |
gene amyX | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.B8 | beta-cyclodextrin + H2O | - |
Bacillus subtilis | maltose + D-glucose | - |
? | |
3.2.1.B8 | beta-cyclodextrin + H2O | - |
Bacillus subtilis 168 | maltose + D-glucose | - |
? | |
3.2.1.B8 | gamma-cyclodextrin + H2O | - |
Escherichia coli K-12 | maltose + D-glucose | - |
? | |
3.2.1.B8 | malto-heptaose + H2O | - |
Bacillus subtilis | maltose + D-glucose | - |
? | |
3.2.1.B8 | malto-heptaose + H2O | - |
Bacillus subtilis 168 | maltose + D-glucose | - |
? | |
3.2.1.B8 | malto-tetraose + H2O | - |
Escherichia coli K-12 | maltose + D-glucose | - |
? | |
3.2.1.B8 | malto-triose + H2O | - |
Escherichia coli K-12 | maltose + D-glucose | - |
? | |
3.2.1.B8 | additional information | MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6 | Bacillus subtilis | ? | - |
? | |
3.2.1.B8 | additional information | MalZ has catalytic characteristics similar to those of MAase, hydrolyzing gamma-CD and attacking maltooligosaccharides from the reducing end, but differs in substrate preference, producing glucose from relatively small maltooligosaccharides, G3 and G4 | Escherichia coli K-12 | ? | - |
? | |
3.2.1.B8 | additional information | MAase hydrolyzes gamma-cyclodextrin and attacks maltooligosaccharides from the reducing end prefering maltoheptaose G7, as well as maltopentaose G5 and maltohexaose G6 | Bacillus subtilis 168 | ? | - |
? | |
3.2.1.41 | additional information | with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX | Bacillus subtilis | ? | - |
? | |
3.2.1.41 | additional information | with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX | Bacillus subtilis 168 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.B8 | MAase | - |
Bacillus subtilis |
3.2.1.B8 | maltogenic amylase | - |
Bacillus subtilis |
3.2.1.B8 | maltogenic amylase | - |
Escherichia coli K-12 |
3.2.1.B8 | MalZ | - |
Escherichia coli K-12 |
3.2.1.B8 | YvdF | - |
Bacillus subtilis |
3.2.1.41 | AmyX | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.1.41 | metabolism | the debranching enzyme pullulanase is involved in the carbohydrate metabolism of Bacillus subtilis | Bacillus subtilis |
3.2.1.41 | physiological function | role of pullulanase in glycogen utilization and the sequential process of glycogen breakdown, overview | Bacillus subtilis |