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Information on EC 3.2.1.14 - chitinase

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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
                3.2.1.14 chitinase
IUBMB Comments
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
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This record set is specific for:
UNIPROT: Q973G3
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
chitinase, chitotriosidase, endochitinase, antifreeze protein, chit1, amcase, chitinase a, exochitinase, acidic mammalian chitinase, class i chitinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STK_09390
locus name
1,4-beta-poly-N-acetylglucosaminidase
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-
-
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beta-1,4-poly-N-acetyl glucosamidinase
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-
-
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CF-AG
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-
-
-
CF-antigen
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-
-
-
CHI-26
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-
-
-
CHIT 1A
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-
-
-
CHIT 1B
-
-
-
-
chitodextrinase-N-
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-
-
-
Complement-fixation antigen
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-
-
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endochitinase
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-
-
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MF1 antigen
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-
-
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poly-beta-glucosaminidase
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-
-
-
UDA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
(1->4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase
The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo-chitodextrinases can act. Activity is greatly stimulated in the presence of EC 1.14.99.53, lytic chitin monoxygenase, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase. cf. EC 3.2.1.202, endo-chitodextrinase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-06-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chitin + H2O
N,N-diacetylchitobiose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
chitin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.075
pH and temperature not specified in the publication, substrate: colloidal chitin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.32
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Y939_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
709
0
77730
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
gel filtration
77000
2 * 77000, SDS-PAGE
77700
2 * 77700, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Staufenberger, T.; Imhoff, J.F.; Labes, A.
First crenarchaeal chitinase found in Sulfolobus tokodaii
Microbiol. Res.
167
262-269
2012
Sulfurisphaera tokodaii (Q973G3), Sulfurisphaera tokodaii
Manually annotated by BRENDA team