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Information on EC 3.4.21.4 - trypsin and Organism(s) Fusarium oxysporum and UniProt Accession P35049

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.4 trypsin
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Select one or more organisms in this record: ?
This record set is specific for:
Fusarium oxysporum
UNIPROT: P35049 not found.
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Word Map
The taxonomic range for the selected organisms is: Fusarium oxysporum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
preferential cleavage: Arg-/-, Lys-/-
Synonyms
trypsin, at-ii, cationic trypsinogen, beta-trypsin, trypsin-like enzyme, mesotrypsin, trypsin a, cationic trypsin, anionic trypsinogen, anionic trypsin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-trypsin
-
-
-
-
Anionic trypsinogen
-
-
-
-
beta-trypsin
-
-
-
-
Brain trypsinogen
-
-
-
-
Cationic trypsinogen
-
-
-
-
cocoonase
-
-
-
-
Mesotrypsinogen
-
-
-
-
parenzyme
-
-
-
-
parenzymol
-
-
-
-
pseudotrypsin
-
-
-
-
SET
-
-
-
-
sperm receptor hydrolase
-
-
-
-
tripcellim
-
-
-
-
tryptar
-
-
-
-
tryptase
-
-
-
-
trypure
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9002-07-7
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Locusta migratoria protease inhibitor 1
-
strong inhibition
-
Locusta migratoria protease inhibitor 3
-
strong inhibition, the inhibitor interacts with trypsin through the reactive site P3-P4' and the P10-P6 residues
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-acetyl-piperazide
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-methylpiperidide
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid methyl ester
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid methylester
-
-
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-piperazide
-
-
napsagatran
-
-
napsagatran ethylester
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00041
CRC 220
-
-
0.000044
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-acetyl-piperazide
-
-
0.000042
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-methylpiperidide
-
-
0.00066
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid
-
-
0.0011
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid methyl ester
-
-
0.00022
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid
-
-
0.000021
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid methylester
-
-
0.00012
Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-piperazide
-
-
0.0116
napsagatran
-
-
0.03
napsagatran ethylester
-
-
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?
TRYP_FUSOX
248
0
24576
Swiss-Prot
Secretory Pathway (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor. Cocrystallization with PMSF or DFP
sitting-drop vapour-diffusion method, X-ray studies of trypsin with its own autolysis products and in presence of the added amino acids arginine, lysine and glutamate
analysis of structures at three different pH-values and two different temperatures, comparison with more trypsin structures
-
in complex with Locusta migratoria protease inhibitor 3, hanging drop vapour diffusion method, using 0.1 M sodium citrate pH 4.9 and 24% PEG 4000
-
vapour diffusion method, crystal structure of the enzyme in complex with 1b, 1cMe, 1d and 1dAc
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rypniewski, W.R.; Ostergaard, P.R.; Norregaard-Madsen, M.; Dauter, M.; Wilson, K.S.
Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding
Acta Crystallogr. Sect. D
57
8-19
2001
Fusarium oxysporum (P35049), Fusarium oxysporum
Manually annotated by BRENDA team
Schmidt, A.; Jelsch, C.; Ostergaard, P.; Rypniewski, W.; Lamzin, V.S.
Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis
J. Biol. Chem.
278
43357-43362
2003
Fusarium oxysporum (P35049)
Manually annotated by BRENDA team
Dullweber, F.; Stubbs, M.T.; Musil, D.; Sturzebecher, J.; Klebe, G.
Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition
J. Mol. Biol.
313
593-614
2001
Fusarium oxysporum
Manually annotated by BRENDA team
Schmidt, A.; Lamzin, V.S.
Extraction of functional motion in trypsin crystal structures
Acta crystallogr. Sect. D
61
1132-1139
2005
Fusarium oxysporum
Manually annotated by BRENDA team
Leone, P.; Roussel, A.; Kellenberger, C.
Structure of Locusta migratoria protease inhibitor 3 (LMPI-3) in complex with Fusarium oxysporum trypsin
Acta Crystallogr. Sect. D
64
1165-1171
2008
Fusarium oxysporum
Manually annotated by BRENDA team