Information on EC 3.4.22.24 - cathepsin T

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Rattus norvegicus

EC NUMBER
COMMENTARY
3.4.22.24
-
RECOMMENDED NAME
GeneOntology No.
cathepsin T
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
interconversion of the three forms of tyrosine aminotransferase, EC 2.6.1.5
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
77464-86-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
albino male Holtzman rats
-
-
Manually annotated by BRENDA team
CCl4-treated rats
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Acid-denatured hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
degradation
-
-
?
Benzoxycarbonyl-Phe-Arg-methylcoumarylamide + H2O
?
show the reaction diagram
-
-
-
-
-
Performic acid-oxidized ribonuclease A + H2O
Hydrolyzed performic acid-oxidized ribonuclease A
show the reaction diagram
-
-
-
-
-
Performic acid-oxidized ribonuclease A + H2O
Hydrolyzed performic acid-oxidized ribonuclease A
show the reaction diagram
-
even at 0C
several fragments
-
Tyrosine aminotransferase + H2O
?
show the reaction diagram
-
involved in generation of isozymic forms of tyrosine transferase
-
-
-
tyrosine aminotransferase + H2O
truncated tyrosine aminotransferase + peptide
show the reaction diagram
-
53 kDa substrate monomer, cleavage at the N-terminus of the protein, interconversion of the 3 different forms of the substrate enzyme without alteration of its enzymatic activity related to the substrate's short half-life in the cell, 53 kDa substrate monomer, cleavage at the N-terminus of the protein, interconversion of the 3 different forms of the substrate enzyme without alteration of its enzymatic activity
49 kDa product monomer and 4.5 kDa N-terminal peptide
-
?
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
-
-
-
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
dimer of MW 52000 subunits
enzyme form II: dimer of MW 53000 + MW 49000, enzyme form III: dimer of MW 48000
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
enzyme converses native larger subunit to smaller subunit
-
-
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
from rat liver cytosol
enzyme form II: dimer of MW 53000 + MW 49000, enzyme form III: dimer of MW 48000
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
from rat liver cytosol
no release of amino acids, amino acid composition of acidic peptide
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
thereby generating multiple forms of tyrosine aminotransferase
-
-
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
thereby generating multiple forms of tyrosine aminotransferase
enzyme form II: dimer of MW 53000 + MW 49000, enzyme form III: dimer of MW 48000
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
thereby generating multiple forms of tyrosine aminotransferase
no release of amino acids, amino acid composition of acidic peptide
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
thereby generating multiple forms of tyrosine aminotransferase
enzyme form III: dimer of MW 49000
-
Tyrosine aminotransferase form I + H2O
Tyrosine aminotransferase form II and III + acidic peptide of MW 4500 peptide
show the reaction diagram
-
i.e. L-tyrosine:2-oxoglutarate aminotransferase or EC 2.6.1.5
enzyme form II: dimer of MW 53000 + MW 49000, enzyme form III: dimer of MW 48000
-
Hemoglobin + H2O
?
show the reaction diagram
-
denaturation
-
-
?
additional information
?
-
-
no hydrolysis of synthetic low MW substrates for exopeptidases, e.g. Gly-(L)-Phe-beta-naphthylamide, L-Ser-(L)-Tyr-beta-naphthylamide, L-Leu-beta-naphthylamide, L-Arg-beta-naphthylamide, L-leucinamide, hippuryl-L-arginine, hippuryl-L-phenylalanine, N-benzoyl-L-tyrosine ethyl ester
-
-
-
additional information
?
-
-
cytosolic or mitochondrial forms of aspartate aminotransferase
-
-
-
additional information
?
-
-
Nalpha-benzoyl-(DL)-Arg-beta-naphthylamide
-
-
-
additional information
?
-
-
little or no activity at 0C with glucose 6-phosphate dehydrogenase, native ribonuclease A, native bovine serum albumin, cytochrome c or oxidized insulin B-chain
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Tyrosine aminotransferase + H2O
?
show the reaction diagram
-
involved in generation of isozymic forms of tyrosine transferase
-
-
-
tyrosine aminotransferase + H2O
truncated tyrosine aminotransferase + peptide
show the reaction diagram
-
53 kDa substrate monomer, cleavage at the N-terminus of the protein, interconversion of the 3 different forms of the substrate enzyme without alteration of its enzymatic activity related to the substrate's short half-life in the cell
49 kDa product monomer and 4.5 kDa N-terminal peptide
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,4'-dipyridyl disulfide
-
-
N-ethylmaleimide
-
-
Oxidized ribonuclease A
-
tyrosine aminotransferase as substrate
-
tosyl-L-lysine chloromethyl ketone
-
-
tosyl-Lys-methylchloride
-
-
Low molecular weight thiol proteinase inhibitor fractions
-
of human or rat serum, human synovial fluid and cerebrospinal fluid, MW 17000
-
additional information
-
no inhibition by native ribonuclease A
-
additional information
-
no inhibition by pepstatin A, soybean trypsin inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation, 4 mM
cysteine
-
activation, 4 mM
DTT
-
activation, 2 mM
EDTA
-
2 mM; activation
EDTA
-
activation
EDTA
-
activates
sulfhydryl compounds
-
activation
GSH
-
activation, 4 mM
additional information
-
carbon tetrachloride induces the enzyme 7fold in the liver
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
-
-
at 0C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
active in this range, negligible below pH 5 and above pH 8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
assay at, tyrosine aminotransferase as substrate
37
-
-
assay at, proteins as substrate
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
high activity
Manually annotated by BRENDA team
-
effect of hepatotoxins, e.g. thiolacetamide or dimethylnitrosamine and partial hepatectomy on cathepsin T activity in rat liver
Manually annotated by BRENDA team
additional information
-
tissue distribution, no activity in heart, skeletal muscle, brain and blood
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
33500
-
-
gel filtration; kidney; rat, liver
33500
-
-
gel filtration; rat, liver
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
kidney; SDS-PAGE
monomer
-
1 * 35000, rat, liver; SDS-PAGE
monomer
-
1 x 35000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
15 min, 37C, 50% loss of activity
7
-
-
above, 0C, 1.25% glycerol, rapid loss of activity
7.8
-
-
20 min, 0C, inactivation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
15 min, pH 6.5, 50% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, in 50 mM sodium phosphate buffer, pH 6.5, 25 mM NaCl, 12.5% glycerol, 1 mM DTT, at least 2 months
-
4C, at somewhat higher ionic strength than 50 mM sodium phosphate, pH 6.5, 25 mM NaCl, 12.5% glycerol, 1 mM DTT, inactivation within 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
kidney; liver
-
native enzyme to homogeneity from liver
-