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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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UNIPROT: Q8U1H5
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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
PF1233
locus name
1,4-beta-poly-N-acetylglucosaminidase
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beta-1,4-poly-N-acetyl glucosamidinase
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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
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chitodextrinase-N-
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Complement-fixation antigen
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endochitinase
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MF1 antigen
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poly-beta-glucosaminidase
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UDA
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-
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
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
show the reaction diagram
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 12.7
4-nitrophenyl beta-N,N'-diacetylchitobioside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 6.7
4-nitrophenyl beta-N,N'-diacetylchitobioside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 14.6
4-nitrophenyl chitobioside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
Q8U1H5_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
717
0
78635
TrEMBL
other Location (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of chitinase recombinantly expressed in Escherichia coli, hanging-drop vapour diffusion method, resolution of 1.50 A. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.0, b = 92.8, c = 107.2 A
hanging drop vapor diffusion method, crystallographic analyses of the catalytic domain of chitinase. Crystals of these mutant enzymes E526A and D524A in complex with chito-oligosaccharide substrate by means of cocrystallization and soaking methods, respectively, and determination of their tertiary structures. X-ray diffraction data are collected, resolutions of 1.80 A and 1.76 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D522A
mutation causes a 7.3fold decrease in kcat/Km for 4-nitrophenyl chitobioside
D522N
mutation causes a 3.4fold decrease in kcat/Km for 4-nitrophenyl chitobioside
D524A
mutation causes a 58.4 fold decrease in kcat/Km for 4-nitrophenyl chitobioside
D524N
mutation causes a 3.6fold decrease in kcat/Km for 4-nitrophenyl chitobioside
E526A
no activity detected with 4-nitrophenyl chitobioside
E526Q
mutation causes a 38.4fold decrease in kcat/Km for 4-nitrophenyl chitobioside
W664A
mutation causes a 8588fold decrease in kcat/Km for 4-nitrophenyl chitobioside
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of chitinase recombinantly expressed in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of wild-type enzyme and mutant enzymes D522N, D522A, D524N, D524A, E526Q and E526A in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mine, S.; Nakamura, T.; Hirata, K.; Ishikawa, K.; Hagihara, Y.; Uegaki, K.
Crystallization and X-ray diffraction analysis of a catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus
Acta Crystallogr. Sect. F
62
791-793
2006
Pyrococcus furiosus (Q8U1H5), Pyrococcus furiosus
Manually annotated by BRENDA team
Tsuji, H.; Nishimura, S.; Inui, T.; Kado, Y.; Ishikawa, K.; Nakamura, T.; Uegaki, K.
Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus - the role of conserved residues in the active site
FEBS J.
277
2683-2695
2010
Pyrococcus furiosus (Q8U1H5), Pyrococcus furiosus
Manually annotated by BRENDA team