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Information on EC 3.4.21.1 - chymotrypsin and Organism(s) Rattus norvegicus and UniProt Accession P07338

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.1 chymotrypsin
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P07338 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage: Tyr-/-, Trp-/-, Phe-/-, Leu-/-
Synonyms
chymotrypsin, alpha-chymotrypsin, bovine alpha-chymotrypsin, chymotrypsin a, alpha-ct, chymotrypsin b, chtp, alpha chymotrypsin, alpha-chymotrypsin a, chymotrypsin ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chymotrypsin B
-
lysosomal Bid cleavage protease
-
alpha chymar
-
-
-
-
alpha-chymar ophth
-
-
-
-
alpha-chymotrypsin
alpha-chymotrypsin A
-
-
-
-
avazyme
-
-
-
-
chymar
-
-
-
-
chymotest
-
-
-
-
chymotrypsin A
-
-
-
-
chymotrypsin B
-
-
-
-
chymotrypsin-B
-
-
EC 3.4.4.6
-
-
-
-
enzeon
-
-
-
-
quimar
-
-
-
-
quimotrase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9004-07-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
BH3 interacting domain death agonist + H2O
?
show the reaction diagram
-
-
-
?
N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Pro-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
preferred substrate
-
-
?
rat chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Tyr + 7-amino-4-methylcoumarin
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
rat chymotrypsinogen + H2O
?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
complete inhibition at 0.2 mM
Aprotinin
partial inhibition at 0.1 mg/ml
chymostatin
complete inhibition at 0.25 mM
N-p-tosyl-L-phenylalanine-chloromethyl ketone
complete inhibition at 5 mM
Phenylmethylsulfonylfluoride
complete inhibition at 2 mM
SERPINB3
partial inhibition
-
SERPINB4
partial inhibition
-
Soybean trypsin inhibitor
complete inhibition at 0.1 mg/ml
-
additional information
not inhibited by benzamide and L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
37°C, pH 8.0
0.012
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
-
37°C, pH 8.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
98.3
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin
-
37°C, pH 8.0
105
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin
-
37°C, pH 8.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
-
using N-succinyl-Ala-Ala-Pro-Phe-7-amido-4-metyhlcoumarin as a substrate
9.5
-
using N-succinyl-Ala-Ala-Pro-Lys-7-amido-4-metyhlcoumarin as a substrate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CTRB1_RAT
263
1
27849
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
autolytic inactivation at autolytic sites Phe114, Tyr146 and Asn147
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 0.1 M HEPES pH 7.0 as precipitant solution containing 30% PEG6000
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F114I
-
autolytic site
Y146H
-
autolytic site
Y146H/N147S
-
autolytic sites, altered routes of autolytic degradation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
-
rapid inactivation above 60°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SB-TI-Sepharose column chromatography
SBTI-Sepharose column chromatography and HiPrep Sephacryl-100 column gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bodi, A.; Kaslik, G.; Venekei, I.; Graf, L.
Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin
Eur. J. Biochem.
268
6238-6246
2001
Rattus norvegicus
Manually annotated by BRENDA team
Matrai, J.; Verheyden, G.; Krueger, P.; Engelborghs, Y.
Simulation of the activation of alpha-chymotrypsin: analysis of the pathway and role of the propeptide
Protein Sci.
13
3139-3150
2004
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Miao, Q.; Sun, Y.; Wei, T.; Zhao, X.; Zhao, K.; Yan, L.; Zhang, X.; Shu, H.; Yang, F.
Chymotrypsin B cached in rat liver lysosomes and involved in apoptotic regulation through a mitochondrial pathway
J. Biol. Chem.
283
8218-8228
2008
Rattus norvegicus (P07338)
Manually annotated by BRENDA team
Jelinek, B.; Katona, G.; Fodor, K.; Venekei, I.; Graf, L.
The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin
Protein J.
27
79-87
2008
Rattus norvegicus
Manually annotated by BRENDA team