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Literature summary for 3.2.1.B8 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)

Cloned (Comment) Organism
expression as malZ-yvdF fusion protein in Escherichia coli strain JT1 Bacillus subtilis
expression as malZ-yvdF fusion protein in Escherichia coli strain JT1 Escherichia coli K-12

Protein Variants

Protein Variants Comment Organism
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
additional information construction of a malZ-yvdF fusion enzyme, substrate specificity, overview Escherichia coli K-12

Localization

Localization Comment Organism GeneOntology No. Textmining
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
-
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

Organism UniProt Comment Textmining
Bacillus subtilis
-
gene yvdF
-
Bacillus subtilis 168
-
gene yvdF
-
Escherichia coli K-12
-
gene malZ
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-cyclodextrin + H2O
-
Bacillus subtilis maltose + D-glucose
-
?
beta-cyclodextrin + H2O
-
Bacillus subtilis 168 maltose + D-glucose
-
?
gamma-cyclodextrin + H2O
-
Escherichia coli K-12 maltose + D-glucose
-
?
malto-heptaose + H2O
-
Bacillus subtilis maltose + D-glucose
-
?
malto-heptaose + H2O
-
Bacillus subtilis 168 maltose + D-glucose
-
?
malto-tetraose + H2O
-
Escherichia coli K-12 maltose + D-glucose
-
?
malto-triose + H2O
-
Escherichia coli K-12 maltose + D-glucose
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?

Synonyms

Synonyms Comment Organism
MAase
-
Bacillus subtilis
maltogenic amylase
-
Bacillus subtilis
maltogenic amylase
-
Escherichia coli K-12
MalZ
-
Escherichia coli K-12
YvdF
-
Bacillus subtilis