Literature summary for 3.2.1.135 extracted from

Majzlova, K.; Pukajova, Z.; Jane?ek, S.
Tracing the evolution of the alpha-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases (2013), Carbohydr. Res., 367, 48-57.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure analysis and modeling of GH13_20 neopullulanase in complex with maltotetraose, PDB ID 1J0J	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	P38940	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyzes the hydrolysis of alpha-1,4- and alpha-1,6-glucosidic linkages (of pullulan) of transglycosylations to form both alpha-1,4- and alpha-1,6-glucosidic bonds	Geobacillus stearothermophilus	?	-	?

General Information

General Information	Comment	Organism
evolution	analysis and verification of neopullulanases belonging to the alpha-amylase family GH13, subfamily GH13_20, but also subfamily GH13_36, an intermediary group, which is defined using the sequence of the fifth conserved sequence region (CSR) as a selection marker. Evolutionary relationships and tree, and conserved sequence regions of GH13 subfamilies, detailed overview. The GH13_20 neopullulanase from Bacillus stearothermophilus in complex with maltotetraose is a representative of the neopullulanase subfamily. One of the most clear sequence signatures of true members of the neopullulanase subfamily subfamily GH13_20 is the stretch VANE succeeding the catalytic nucleophile in the CSR II, although not every GH13_20 member has to possess this segment in its entirety. GH13_36 enzymes contain a histidine at the end of the CSR II (strand beta4) and a tryptophan (or at least an aromatic residue) two residues succeeding the catalytic proton donor in the CSR III (strand beta5)	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)