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Information on EC 3.2.1.41 - pullulanase and Organism(s) Klebsiella pneumoniae and UniProt Accession P07206

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.41 pullulanase
IUBMB Comments
Different from EC 3.2.1.142 (limit dextrinase) 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.
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This record set is specific for:
Klebsiella pneumoniae
UNIPROT: P07206
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The taxonomic range for the selected organisms is: Klebsiella pneumoniae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pullulanase, debranching enzyme, amylopullulanase, pulask, r-enzyme, pullulanase type i, pbpula, bapul13a, type ii pullulanase, pulwb42, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
Alpha-dextrin endo-1,6-alpha-glucosidase
-
-
-
-
amylopectin 6-glucanohydrolase
-
-
-
-
glucanohydrolase, amylopectin 6-
-
-
-
-
limit dextrinase
-
-
-
-
Pullulan 6-glucanohydrolase
-
-
-
-
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
R-enzyme
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
pullulan 6-alpha-glucanohydrolase
Different from EC 3.2.1.142 (limit dextrinase) 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.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-68-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
maltooligosaccharides + maltose
show the reaction diagram
pullulan + H2O
maltotriose + ?
show the reaction diagram
-
-
-
-
?
soluble starch
maltotriose + maltose
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
maltooligosaccharides + maltose
show the reaction diagram
-
branched polysaccharides
-
-
?
pullulan + H2O
maltotriose + ?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the Klebsiella lipoprotein pullulanase (PulA) is exported to the periplasm, triacylated, and anchored via lipids in the inner membrane prior to its transport to the bacterial surface through a type II secretion system
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PULA_KLEPN
1090
0
118098
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000 - 116000
-
mature protein
118000
-
precursor protein, gel electrophoresis, amino acid analysis
120000
-
SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method. Characterization of the Ins subdomain by X-ray crystallography
hanging-drop vapour-diffusion method, crystal structure of pullulanase and its complex with glucose, maltose, isomaltose, maltotriose and maltotetraose, 1.7-1.9 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 11
-
-
136430
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pugsley, A.P.; Chapon, C.; Schwartz, M.
Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein
J. Bacteriol.
166
1083-1088
1986
Klebsiella pneumoniae
Manually annotated by BRENDA team
Michaelis, S.; Chapon, C.; d'Enfert, C.; Pugsley, A.P.; Schwartz, M.
Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
J. Bacteriol.
164
633-638
1985
Klebsiella pneumoniae
Manually annotated by BRENDA team
Kornacker, M.G.; Pugsley, A.P.
Molecular characterization of pulA and its product, pullulanase, a secreted enzyme of Klebsiella pneumoniae UNF5023
Mol. Microbiol.
4
73-85
1989
Klebsiella pneumoniae, Klebsiella pneumoniae UNF5023
Manually annotated by BRENDA team
Yamashita, M.; Nakagawa, A.; Katsuragi, N.; Murooka, Y.
Role of lipid modification on a starch-debranching enzyme, Klebsiella pullulanase: comparison of properties of lipid-modified and unmodified pullulanases
Mol. Microbiol.
6
389-394
1992
Klebsiella aerogenes, Klebsiella pneumoniae
Manually annotated by BRENDA team
Mikami, B.; Iwamoto, H.; Malle, D.; Yoon, H.J.; demirkan-Sarikaya, E.; Mezaki, Y.; Katsuya, Y.
Crystal structure of pullulanase: evidence for parallel binding of oligosacchjarides in the active site
J. Mol. Biol.
359
690-707
2006
Klebsiella pneumoniae
Manually annotated by BRENDA team
East, A.; Mechaly, A.E.; Huysmans, G.H.M.; Bernarde, C.; Tello-Manigne, D.; Nadeau, N.; Pugsley, A.P.; Buschiazzo, A.; Alzari, P.M.; Bond, P.J.; Francetic, O.
Structural basis of pullulanase membrane binding and secretion revealed by X-Ray crystallography, molecular dynamics and biochemical analysis
Structure
24
92-104
2016
Klebsiella pneumoniae (P07206)
Manually annotated by BRENDA team