Information on EC 3.4.23.B1 - napsin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
napsin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
belongs to the aspartic proteinases
show the reaction diagram
proteolytic cleavage of polypeptides to large and stable peptides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
208934-04-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
K(dabsyl)-TSLLMAAPQ-Lucifer yellow (DS1) + H2O
?
show the reaction diagram
K(dabsyl)-TSVLMAAPQ-Lucifer yellow (DS3) + H2O
?
show the reaction diagram
polypeptide + H2O
peptides
show the reaction diagram
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
show the reaction diagram
pulmonary surfactant protein B + H2O
?
show the reaction diagram
pulmonary surfactant protein C + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
K(dabsyl)-TSLLMAAPQ-Lucifer yellow (DS1) + H2O
?
show the reaction diagram
-
-
-
-
-
polypeptide + H2O
peptides
show the reaction diagram
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
show the reaction diagram
-
napsin A is involved in the N- and C-terminal processing of proSP-B in type II pneumocytes
-
-
-
pulmonary surfactant protein B + H2O
?
show the reaction diagram
pulmonary surfactant protein C + H2O
?
show the reaction diagram
-
napsin A is involved in the post-translational processing of pulmonary surfactant protein B and C in multivesivular bodies of type II pneumocytes
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17 kDa protein of Ascaris lumbricoides
-
weak inhibition
-
ABT-538
-
HIV proteinase inhibitor
Ac-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
-
ethoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
-
isobutyryl-HPFA-statine-LF-NH2
-
-
isobutyryl-HPFH-statine-LF-NH2
-
-
isobutyryl-HPFY-statine-LF-NH2
-
-
isovaleryl-HPF-2-naphthylalanine-statine-LF-NH2
-
-
isovaleryl-HPF-homophenylalanine-statine-LF-NH2
-
-
isovaleryl-HPFH-(4-amino-3-hydroxy-5-phenylpentanoic acid)-LF-NH2
-
-
isovaleryl-HPFH-(4-amino-3-hydroxy-6-methylheptanoic acid)-LF-NH2
-
-
isovaleryl-HPFH-statine-delta-N-acetylornithine-F-NH2
-
-
isovaleryl-HPFH-statine-IF-NH2
-
-
isovaleryl-HPFH-statine-IH-NH2
-
-
isovaleryl-HPFH-statine-LF-NH2
-
-
isovaleryl-pepstatin
-
strong inhibition
-
Lactoyl-pepstatin
-
strong inhibition
-
Pepstatin
t-butoxycarbonyl-HPFH-statine-LF-NH2
-
-
t-butoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
-
t-butoxycarbonyl-Phe-His-statine-Leu-Phe-NH2
-
-
TLIRIPLHRVQPGRRILNL
-
biotinylated, derived from residues 1P-19P of the 34 amino acid propart of pronapsin A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
K(dabsyl)-TSLLMAAPQ-Lucifer yellow (DS1)
-
pH 4.7, 25C
0.0062
K(dabsyl)-TSVLMAAPQ-Lucifer yellow (DS3)
-
pH 4.7, 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
17 kDa protein of Ascaris lumbricoides
-
pH 4.7, 37C
-
0.00011
ABT-538
-
pH 4.7, 37C
0.00001
Ac-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
pH 4.7, 37C
0.00002
ethoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
pH 4.7, 37C
0.00007
isobutyryl-HPFA-statine-LF-NH2
-
pH 4.7, 37C
0.00016
isobutyryl-HPFH-statine-LF-NH2
-
pH 4.7, 37C
0.001
isobutyryl-HPFY-statine-LF-NH2
-
pH 4.7, 37C
0.000105
isovaleryl-HPF-2-naphthylalanine-statine-LF-NH2
-
pH 4.7, 37C
0.000003
isovaleryl-HPF-homophenylalanine-statine-LF-NH2
-
pH 4.7, 37C
0.000012
isovaleryl-HPFH-(4-amino-3-hydroxy-5-phenylpentanoic acid)-LF-NH2
-
pH 4.7, 37C
0.000065
isovaleryl-HPFH-(4-amino-3-hydroxy-6-methylheptanoic acid)-LF-NH2
-
pH 4.7, 37C
0.00014
isovaleryl-HPFH-statine-delta-N-acetylornithine-F-NH2
-
pH 4.7, 37C
0.000055
isovaleryl-HPFH-statine-IF-NH2
-
pH 4.7, 37C
0.00057
isovaleryl-HPFH-statine-IH-NH2
-
pH 4.7, 37C
0.0002
isovaleryl-HPFH-statine-LF-NH2
-
pH 4.7, 37C
0.00000015
isovaleryl-pepstatin
-
pH 4.7, 37C
-
0.000016
Lactoyl-pepstatin
-
pH 4.7, 37C
-
0.000002
Pepstatin
0.003
t-butoxycarbonyl-HPFH-statine-LF-NH2
-
pH 4.7, 37C
0.000185
t-butoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
pH 4.7, 37C
0.000012
t-butoxycarbonyl-Phe-His-statine-Leu-Phe-NH2
-
pH 4.7, 37C
0.0005
TLIRIPLHRVQPGRRILNL
-
pH 4.7, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5.5
-
recombinant enzyme, at room temperature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.29
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in pleural effusions
Manually annotated by BRENDA team
-
bronchoalveolar lavage fluid (BALF), expression in
Manually annotated by BRENDA team
-
re-expression of napsin A in tumorigenic HEK293 kidney cell line, reduced capacity for anchorage-independent growth observed
Manually annotated by BRENDA team
-
of peripheral blood
Manually annotated by BRENDA team
-
weak detection of napsin A in cytoplasm of lung sarcomatoid carcinoma cells
Manually annotated by BRENDA team
-
enzymatically active napsin A can be detected in urine of healthy individuals or in patients with transplanted kidney whose kidney function appears half to fully normal. Low activity in samples from patients with diseased kidneys
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
x * 37000, deglycosylated protein, SDS-PAGE
38000
-
x * 38000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 39000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
napsin A is expressed as preproenzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
half-life more than 10 h
668762
5
-
10 h, 37C, stable
658595
6
-
10 h, 37C, stable
658595
7
-
half-life is around 4 h
668762
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant from HEK-293 cells, to homogeneity, 1-step procedure with propeptide of napsin A as affinity ligand
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in HEK-293 cells
DNA sequence determination and analysis, expression in HEK-293 cells; DNA sequence determination and analysis, expression in HEK-293 cells
-
expression in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
napsin-A is decreased in stage IIIA primary lesions, napsin-A shows reduced expression in both IIIA primary sites and IIIA lymph nodes
-
napsin-A is highly expressed in stage IA primary lesions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine