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Information on EC 3.2.1.14 - chitinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P29029

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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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Saccharomyces cerevisiae
UNIPROT: P29029
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected 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
1,4-beta-poly-N-acetylglucosaminidase
-
-
-
-
beta-1,4-poly-N-acetyl glucosamidinase
-
-
-
-
CF-AG
-
-
-
-
CF-antigen
-
-
-
-
CHI-26
-
-
-
-
CHIT 1A
-
-
-
-
CHIT 1B
-
-
-
-
chitodextrinase-N-
-
-
-
-
Complement-fixation antigen
-
-
-
-
endochitinase
-
-
-
-
MF1 antigen
-
-
-
-
poly-beta-glucosaminidase
-
-
-
-
UDA
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-N,N',N''-triacetylchitotriose + H2O
?
show the reaction diagram
-
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
show the reaction diagram
-
nascent more effectively than preformed chitin
chitobiose and a small amount of chitotriose only
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-chlorotheophylline
-
acetazolamide
competitive
kinetin
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 1.1
4-methylumbelliferyl-N,N',N''-triacetylchitotriose
3.9
chitin
-
expressed in N-acetylglucosamine equivalents
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 2.3
4-methylumbelliferyl-N,N',N''-triacetylchitotriose
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.192
8-chlorotheophilline
mutant enzyme F210W/A283S
0.6 - 1.155
8-chlorotheophylline
0.021 - 0.128
acetazolamide
0.00061 - 0.00146
allosamidin
0.0032
kinetin
wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.6
substrate: 4-methylumbelliferyl-N,N',N''-triacetylchitotriose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 4
pH 2: about 80% of maximal activity, pH 4.0: about 55% of maximal activity, substrate: 4-methylumbelliferyl-N,N',N''-triacetylchitotriose
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the native enzyme and the enzyme in complex with 8-chlorotheophylline, kinetin or acetazolamide, sitting drop method, 1.6 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A283S
Km-value for mutant enzyme for 4-methylumbelliferyl-N,N',N''-triacetylchitotriose is 0.8 mM versus 1 mM for wild-type enzyme and turnover number is 2.3 per sec versus 1.3 for wild-type enzyme. Inhibition by allosamidin, acetazolamide, and 8-chlorotheophylline are not significantly affected by the mutation, inhibition by kinetin is not detectable
F210W/A283S
similar Km (1.1 versus 1 mM for wild-type) and turnover number kcat (0.8 versus 1.3 for wild-type) as for the wild-type enzyme and the single A283S mutant. Inhibition by allosamidin, acetazolamide, and 8-chlorotheophylline is not significantly affected by the mutation, inhibition by kinetin is not detectable
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, 2 months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the catalytic domain of ScCTS1 (comprising of amino acids 22 to 315) as a secreted N-terminally His-tagged fusion protein in Pichia pastoris
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Correa, J.U.; Elango, N.; Polacheck, I.; Cabib, E.
Endochitinase, a mannan-associated enzyme from Saccharomyces cerevisiae
J. Biol. Chem.
257
1392-1397
1982
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hurtado-Guerrero, R.; van Aalten, D.M.
Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitors
Chem. Biol.
14
589-599
2007
Saccharomyces cerevisiae (P29029), Saccharomyces cerevisiae
Manually annotated by BRENDA team