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Literature summary extracted from

  • Shim, J.H.; Park, J.T.; Hong, J.S.; Kim, K.W.; Kim, M.J.; Auh, J.H.; Kim, Y.W.; Park, C.S.; Boos, W.; Kim, J.W.; Park, K.H.
    Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168 (2009), J. Bacteriol., 191, 4835-4844.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

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

Localization

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
-
-

Organism

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
-

Substrates and Products (Substrate)

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 ?
-
 ?

Synonyms

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

General Information

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