Pullulanase
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A Pullulanase is a Glucanase, an Amylolytic Exoenzyme, that degrades Pullulan.
- AKA: Pullulan-6-Glucanohydrolase, Alpha-Dextrin Endo-1,6-Alpha-Glucosidase, Amylopectin 6-Glucanohydrolase, Debranching Enzyme, Limit Dextrinase.
- Context:
- It can hydrolytically cleave pullulan.
- It can be identified as following enzyme entry: EC 3.2.1.41.
- Example(s):
- Klebsiella pneumoniae http://www.uniprot.org/uniprot/P07206
- PMID 3322811: “The protein concerned, pullulanase, is a secreted lipoprotein of the Gram-negative bacterium Klebsiella pneumoniae.”
- Counter-Example(s):
- See: Gram-Negative Bacteria, Klebsiella.
References
2019a
- (Wikipedia, 2019) ⇒ https://en.wikipedia.org/wiki/Pullulanase Retrieved:2019-3-28.
- Pullulanase (EC 3.2.1.41, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, alpha-dextrin endo-1,6-alpha-glucosidase, R-enzyme, pullulan alpha-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella. Type I pullulanases specifically attack α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages. It is also produced by some other bacteria and archaea. Pullulanase is used as a processing aid in grain processing biotechnology (production of ethanol and sweeteners).
Pullulanase is also known as pullulan-6-glucanohydrolase (Debranching enzyme). Its substrate, pullulan, is regarded as a chain of maltotriose units linked by alpha-1,6-glycosidic bonds. Pullulanase will hydrolytically cleave pullulan (alpha-glucan polysaccharides).
- Pullulanase (EC 3.2.1.41, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, alpha-dextrin endo-1,6-alpha-glucosidase, R-enzyme, pullulan alpha-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella. Type I pullulanases specifically attack α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages. It is also produced by some other bacteria and archaea. Pullulanase is used as a processing aid in grain processing biotechnology (production of ethanol and sweeteners).
201b
- (EC, 2019) ⇒ Retrieved:2019-3-28.
- QUOTE: Reaction catalysed
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen
Comment(s)
- Different from EC 3.2.1.142 in its action on glycogen, and its rate of hydrolysis of limit dextrins.
- Its action on amylopectin is complete.
- Maltose is the smallest sugar that it can release from an [[alpha- (1->6)-linkage]].
- Formerly EC 3.2.1.69.
- QUOTE: Reaction catalysed
2009
- Gene Ontology ⇒ http://amigo.geneontology.org/cgi-bin/amigo/term-details.cgi?term=GO:0004629&session_id=5828amigo1240506945
- Accession: GO:0051060
- Ontology: molecular function
- Synonyms
- related: bacterial debranching enzyme
- related: R-enzyme
- exact: alpha-dextrin endo-1,6-alpha-glucosidase activity
- exact: amylopectin 6-glucanohydrolase activity
- exact: pullulan 6-glucanohydrolase activity
- exact: pullulan alpha-1,6-glucanohydrolase activity
- broad: debranching enzyme activity
- broad: limit dextrinase (erroneous)
- Definition
- Catalysis of the hydrolysis of (1,6)-a-D-glucosidic linkages in pullulan [a linear polymer of a-(1,6)-linked maltotriose units] and in amylopectin and glycogen, and the a- and b-limit dextrins of amylopectin and glycogen. [source: EC:3.2.1.41]