Information on EC 3.4.11.6 - aminopeptidase B

New: Word Map on EC 3.4.11.6
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: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.4.11.6
-
RECOMMENDED NAME
GeneOntology No.
aminopeptidase B
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
-
-
-
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrates possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
exopeptidase, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrate possessing Pro at the P1 position
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
show the reaction diagram
exopeptidase, no endoprotease activity, the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with substrates possessing Pro at the P1 position
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AAP
Debaryomyces hansenii CECT 12487
-
-
-
aminopeptidase B
-
-
aminopeptidase B
-
-
aminopeptidase, arginine
-
-
-
-
aminopeptidase-B
-
-
Ap-B
-
-
Arg/Lys aminopeptidase
-
Arg/Lys aminopeptidase
-
-
arginine aminopeptidase
-
-
-
-
arginine aminopeptidase
-
-
arginine aminopeptidase
-
-
arginine aminopeptidase
-
-
arginine-aminopeptidase
-
-
arginyl aminopeptidase
-
-
-
-
arginyl aminopeptidase
-
-
arginyl aminopeptidase
-
-
arginyl aminopeptidase
Debaryomyces hansenii CECT 12487
-
-
-
arginyl aminopeptidase
-
-
arginyl aminopeptidase
-
-
arginyl peptidase
-
-
arylamidase
-
-
arylamidase II
-
-
-
-
chloride-dependent-basic aminopeptidase
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
Cl--activated arinine aminopeptidase
-
-
Co(II)-Ap-B
-
metal-substituted derivative of Ap-B
cold-active aminopeptidase
-
-
Cu(II)-Ap-B
-
metal-substituted derivative of Ap-B
cytosol aminopeptidase
-
-
-
-
cytosol aminopeptidase IV
-
-
DAP BII
Pseudoxanthomonas mexicana WO24
-
-
dipeptidyl aminopeptidase BII
-
dipeptidyl aminopeptidase BII
Pseudoxanthomonas mexicana WO24
-
-
double-zinc aminopeptidase
-
L-arginine aminopeptidase
-
-
-
-
leukocyte-derived arginine aminopeptidase
-
-
leukocyte-derived arginine aminopeptidase
-
protease IV
-
-
pumAPE
-
-
RAP
Streptococcus gordonii FSS2
-
-
lysine-specific aminopeptidase
-
-
additional information
-
the enzyme belongs to the M1 peptidase family
additional information
-
the enzyme belongs to the M1 peptidase family
additional information
-
the enzyme belongs to the M1 peptidase family
additional information
-
the enzyme belongs to the M1 peptidase family
additional information
-
the enzyme belongs to the M1 peptidase family, and is distinct from the leukotriene A4 hydrolase, bleomycin hydrolase, and puromycin-sensitive aminopeptidase
CAS REGISTRY NUMBER
COMMENTARY
9073-92-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ywad gene
SwissProt
Manually annotated by BRENDA team
strain ATCC 51502
-
-
Manually annotated by BRENDA team
marine psychrophile, strain 34H
-
-
Manually annotated by BRENDA team
Corycaeus anglicus
-
-
-
Manually annotated by BRENDA team
strain CECT 12487
-
-
Manually annotated by BRENDA team
Debaryomyces hansenii CECT 12487
strain CECT 12487
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene rnpep
-
-
Manually annotated by BRENDA team
rainbow trout
-
-
Manually annotated by BRENDA team
var. Alaska
-
-
Manually annotated by BRENDA team
strains ATCC 27853 and ATCC 33348
-
-
Manually annotated by BRENDA team
Pseudoxanthomonas mexicana WO24
-
SwissProt
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
Wistar rats, gene Ap-B
Uniprot
Manually annotated by BRENDA team
male gilthead sea bream
-
-
Manually annotated by BRENDA team
Streptococcus gordonii FSS2
FSS2
SwissProt
Manually annotated by BRENDA team
Streptococcus sanguinis 903
903
-
-
Manually annotated by BRENDA team
haploid fungus, strain FB1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
when murine ACE2 is given to mice for 4 weeks, a marked increase in serum ACE2 activity is detected. ACE2 leads to the dissipation of Ang II with formation of Ang (1-7)
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-2-naphthylamide + H2O
Ala + 2-naphthylamine
show the reaction diagram
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
-
4.6% of the activity with Leu-4-nitroanilide
-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
show the reaction diagram
Pseudoxanthomonas mexicana, Pseudoxanthomonas mexicana WO24
-
-
?
alpha-Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
show the reaction diagram
-
564% of the activity with Leu-4-nitroanilide
-
?
angiotensin III + H2O
angiotensin IV + ?
show the reaction diagram
-
-
-
?
Arg 4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
2.5% of the activity with Leu-4-nitroanilide
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
as active as Arg-7-amido-4-methylcoumarin
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
Streptococcus gordonii FSS2
-
-
?
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
Arg-7-amido-4-methylcoumarin + H2O
Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Arg-Ala + H2O
Arg + Ala
show the reaction diagram
-
82% of the activity with Arg-Arg
-
?
Arg-alpha-atrial natriuretic factor1-20 + H2O
Arg + alpha-atrial natriuretic factor1-20
show the reaction diagram
-
-
-
?
Arg-Arg + H2O
Arg + Arg
show the reaction diagram
-
-
-
?
Arg-Asp + H2O
Arg + Asp
show the reaction diagram
-
25% of the activity with Arg-Arg
-
?
Arg-beta-atrial natriuretic factor1-20 + H2O
Arg + beta-atrial natriuretic factor1-20
show the reaction diagram
-
-
-
?
Arg-beta-naphthylamide + H2O
L-arginine + 2-naphthylamine
show the reaction diagram
-
substrate used in the activity assay
-
?
Arg-Gly + H2O
Arg + Gly
show the reaction diagram
-
-
?
Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro + H2O
Arg + Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro
show the reaction diagram
i.e. fibronectin-binding inhibitor
-
?
Arg-Gly-Glu-Ser + H2O
Arg + Gly-Glu-Ser
show the reaction diagram
i.e. platelet aggregation inhibitor
-
?
Arg-Gly-Pro-Phe-Pro-Ile + H2O
Arg + Gly-Pro-Phe-Pro-Ile
show the reaction diagram
i.e. sexual agglutination peptide
-
?
Arg-Gly-Tyr-Ala-Leu-Gly + H2O
Arg + Gly-Tyr-Ala-Leu-Gly
show the reaction diagram
-
-
-
?
Arg-Ile + H2O
Arg + Ile
show the reaction diagram
-
32% of the activity with Arg-Arg
-
?
Arg-Leu + H2O
Arg + Leu
show the reaction diagram
-
25% of the activity with Arg-Arg
-
?
Arg-Leu-enkephalin + H2O
Arg + Leu-enkephalin
show the reaction diagram
-
-
-
?
Arg-Leu-enkephalin + H2O
Arg + Leu-enkephalin
show the reaction diagram
-
-
-
?
Arg-Lys + H2O
Arg + Lys
show the reaction diagram
-
88% of the activity with Arg-Arg
-
?
Arg-Lys-Asp-Val-Tyr-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Lys-somatostatin-14 + H2O
Arg + Lys + somatostatin-14
show the reaction diagram
-
sequential removal of basic N-terminal residues
-
?
Arg-Lys-somatostatin-14 + H2O
Arg-Lys + somatostatin-14
show the reaction diagram
-
-
-
?
Arg-Met-enkephalin + H2O
Arg + Met-enkephalin
show the reaction diagram
-
-
-
?
Arg-Met-enkephalin + H2O
Arg + Met-enkephalin
show the reaction diagram
-
-
-
?
Arg-Met-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-neurokinin A + H2O
Arg + neurokinin A
show the reaction diagram
-
-
-
?
Arg-neurokinin A + H2O
Arg + neurokinin A
show the reaction diagram
-
-
-
?
Arg-peptides + H2O
?
show the reaction diagram
-
-
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
or Lys-peptides, metabolism of kinin
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
takes part in later stages of protein degradation in chloroplasts
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
attribution to inflammatory and wound healing processes
-
-
-
Arg-Phe + H2O
Arg + Phe
show the reaction diagram
-
-
?
Arg-Phe + H2O
Arg + Phe
show the reaction diagram
-
35% of the activity with Arg-Arg
-
?
Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val + H2O
Arg + Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val
show the reaction diagram
i.e. protein kinase C substrate
-
?
Arg-Pro + H2O
Arg + Pro
show the reaction diagram
Streptococcus gordonii, Streptococcus gordonii FSS2
-
-
?
Arg-Pro-Lys-Pro-Gln-Gly-Leu-Met + H2O
Arg + Pro-Lys-Pro-Gln-Gly-Leu-Met
show the reaction diagram
i.e. substance P
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg + Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
show the reaction diagram
Streptococcus gordonii, Streptococcus gordonii FSS2
i.e. bradykinin
-
?
Arg-Tyr-Leu-Pro-Thr + H2O
Arg + Tyr-Leu-Pro-Thr
show the reaction diagram
-
proctolin
-
?
Arg-Val-Tyr-Ile-His-Pro-Ile + H2O
Arg + Val-Tyr-Ile-His-Pro-Ile
show the reaction diagram
i.e. angiotensin III
-
?
Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
Arg + Val-Tyr-Ile-His-Pro-Phe
show the reaction diagram
-
angiotensin III
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
protein fragments of azocasein of MW 71 kDa, 83 kDa, and 22 kDa
show the reaction diagram
-
-
-
?
benzoyl-Arg-p-nitroanilide + H2O
benzoyl-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
Cys-Gly + H2O
Cys + Gly
show the reaction diagram
-
4210% of the activity with Leu-4-nitroanilide
-
?
elastin Congo red + H2O
?
show the reaction diagram
-
-
-
-
?
glucagon + H2O
miniglucagon + ?
show the reaction diagram
-
-
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
show the reaction diagram
-
1% activity compared to L-Lys-2-naphthylamide
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
show the reaction diagram
-
less than 0.02% activity compared to L-Arg-2-naphthylamide
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
1.3% of the activity with Leu-4-nitroanilide
-
?
Gly-L-Pro-2-naphthylamide + H2O
Gly-L-Pro + 2-naphthylamine
show the reaction diagram
-
1% activity compared to L-Lys-2-naphthylamide
-
?
Gly-Phe 4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
show the reaction diagram
Pseudoxanthomonas mexicana, Pseudoxanthomonas mexicana WO24
-
-
?
kallidin + H2O
?
show the reaction diagram
-
-
-
-
?
kallidin-10 + H2O
Lys + bradykinin
show the reaction diagram
-
-
-
?
kallidin-10 + H2O
Lys + bradykinin
show the reaction diagram
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
show the reaction diagram
-
0.1% activity compared to L-Arg-2-naphthylamide
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
show the reaction diagram
-
83% activity compared to L-Lys-2-naphthylamide
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
best substrate
-
?
L-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
L-Ala-Ala-Pro-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Arg 7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate, best substrate
-
?
L-Arg-(Met)enkephalin + H2O
L-Arg + (Met)enkephalin
show the reaction diagram
-
-
-
?
L-Arg-(Met)enkephalin + H2O
L-Arg + (Met)enkephalin
show the reaction diagram
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
100% activity
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
show the reaction diagram
-
17% activity compared to L-Lys-2-naphthylamide
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
best substrate
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
best substrate
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
high activity
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
100% activity
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
100% activity
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Debaryomyces hansenii CECT 12487
-
-
-
?
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
L-Arg-peptide + H2O
L-Arg + peptide
show the reaction diagram
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptides
-
?
L-arginine-2-naphthylamide + H2O
2-naphthylamine + L-Arg
show the reaction diagram
-
assay at 37C
-
?
L-arginine-2-naphthylamide + H2O
2-naphthylamine + L-Arg
show the reaction diagram
-
assay at 37C
-
?
L-Asn-7-amido-4-methylcoumarin + H2O
L-Asn + 7-amino-4-methylcoumarin
show the reaction diagram
53% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
15% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-beta-Asn-2-naphthylamide + H2O
L-beta-Asn + 2-naphthylamine
show the reaction diagram
-
9% activity compared to L-Lys-2-naphthylamide
-
?
L-Cys-2-naphthylamide + H2O
L-Cys + 2-naphthylamine
show the reaction diagram
-
1% activity compared to L-Lys-2-naphthylamide
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
show the reaction diagram
-
5% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Gly-L-Arg-2-naphthylamide + H2O
L-Gly-L-Arg + 2-naphthylamine
show the reaction diagram
-
250% activity compared to L-Lys-2-naphthylamide
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
show the reaction diagram
-
15% activity compared to L-Lys-2-naphthylamide
-
?
L-Leu 7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
show the reaction diagram
-
31% activity compared to L-Lys-2-naphthylamide
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
28% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Lys-(Met)enkephalin + H2O
L-Lys + (Met)enkephalin
show the reaction diagram
-
-
-
?
L-Lys-(Met)enkephalin + H2O
L-Lys + (Met)enkephalin
show the reaction diagram
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
100% activity
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
41% activity compared to L-Arg-2-naphthylamide
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
10% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
17% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Lys-L-Ala-2-naphthylamide + H2O
L-Lys-L-Ala + 2-naphthylamine
show the reaction diagram
-
7% activity compared to L-Lys-2-naphthylamide
-
?
L-Lys-p-nitroanilide + H2O
L-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-peptide + H2O
L-Lys + peptide
show the reaction diagram
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptide
-
?
L-lysine-2-naphthylamide + H2O
2-naphthylamine + L-Lys
show the reaction diagram
-
assay at 37C
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
show the reaction diagram
-
-
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
show the reaction diagram
-
2% activity compared to L-Lys-2-naphthylamide
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
19% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
show the reaction diagram
-
0.171% activity compared to L-Arg-2-naphthylamide
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
low activity
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
2% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
7% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
15% activity compared to L-Arg-7-amido-4-methylcoumarin
-
?
L-Tyr 7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
show the reaction diagram
-
0.171% activity compared to L-Arg-2-naphthylamide
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
show the reaction diagram
-
62% activity compared to L-Lys-2-naphthylamide
-
?
L-Val-2-naphthylamide + H2O
L-Val + 2-naphthylamine
show the reaction diagram
-
0.034% activity compared to L-Arg-2-naphthylamide
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
show the reaction diagram
low activity
-
?
Leu-2-naphthylamide + H2O
Leu + 2-naphthylamine
show the reaction diagram
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
7% of the activity with Arg-4-nitroanilide
-
?
Leu-Gly + H2O
Leu + Gly
show the reaction diagram
-
1200% of the activity with Leu-4-nitroanilide
-
?
leukotriene A4 + H2O
L-Arg + leukotriene B4
show the reaction diagram
-
weak in vitro activity
-
?
leukotriene A4 + H2O
L-Arg + leukotriene B4
show the reaction diagram
-
weak in vitro activity
-
?
leukotriene A4 + H2O
leukotriene B4 + ?
show the reaction diagram
-
has a residual catalytic ability to hydrolyze leukotriene A4
-
?
Lys 4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
show the reaction diagram
-
-
-
?
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
-
3.6% of the activity with Arg-7-amido-4-methylcoumarin
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
5% of the activity with Arg-4-nitroanilide
-
?
Lys-7-amido-4-methylcoumarin + H2O
Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
4.3% of the activity with Arg-7-amido-4-methylcoumarin
-
?
Lys-Ala + H2O
Lys + Ala
show the reaction diagram
-
88% of the activity with Arg-Arg
-
?
Lys-Leu-2-naphthylamide + H2O
Lys + Leu-2-naphthylamide
show the reaction diagram
-
-
-
?
Lys-Lys + H2O
Lys + Lys
show the reaction diagram
-
30% of the activity with Arg-Arg
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
show the reaction diagram
-
40.6% of the activity with Leu-4-nitroanilide
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + p-nitroaniline
show the reaction diagram
-
-
-
?
N-succinyl-Gly-Pro-Leu-Gly-Pro 7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate
-
?
Poly-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
thymopentin + H2O
?
show the reaction diagram
-
-
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
show the reaction diagram
-
1.2% of the activity with Leu-4-nitroanilide
-
?
Met-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no hydrolysis of amino acids with apolar groups, without free alpha-amino group, or anionic amino acids
-
-
-
additional information
?
-
-
no activity with Ala-Ala, Ala-Lys, Asp-Ala, Gly-Ala and Leu-Ala. The enzyme exclusively hydrolyzes basic amino acids from the amino termini of peptide substrates. The nature of the amino acid residue at the C-terminus of the dipeptide has an effect on hydrolysis rate. The activity is maximal towards dipeptides with Arg, Lys, or Ala as the C-terminal residue
-
-
?
additional information
?
-
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site
-
-
?
additional information
?
-
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
-
?
additional information
?
-
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
-
?
additional information
?
-
the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
-
-
-
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
-
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
-
additional information
?
-
substrate specificity, 4-nitroanilides of Gly, Glu, Asp, Phe, Pro, and Ala-Pro are poor substrates, overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with benzoyl-Arg-2-naphthylamide, and 2-naphthylamides of Glu, Ser, and Tyr, no activity with Phe-Phe-Ala-2-naphthylamide, Leu-Gly-Gly-4-methoxy-2-naphthylamide, and Gly-Pro-Leu-2-naphthylamide, overview
-
-
-
additional information
?
-
-
substrate specificity, no activity with L-Pro-7-amido-4-methylcoumarin and L-Asp-7-amido-4-methylcoumarin, L-Ser-7-amido-4-methylcoumarin is a poor substrate, overview
-
-
-
additional information
?
-
-
substrate specificity, the enzyme prefers Arg or Lys in N-terminal position, no activity with dipeptide-4-nitroanilides, overview
-
-
-
additional information
?
-
the enzyme catalyzes the N-terminal cleavage of basic residues of peptide or protein substrates
-
-
-
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with bradykinin, neurotensin precursor and substance P, no activity with substrate possessing Pro at the P1 position
-
-
-
additional information
?
-
-
the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides, no activity with substrate possessing Pro at the P1 position
-
-
-
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins
-
-
-
additional information
?
-
-
the enzyme is strictly specific for the removal of N-terminal basic residues from peptides and proteins, no activity with bradykinin, no activity with substrate possessing Pro at the P1 position
-
-
-
additional information
?
-
-
no activity with L-Ala-7-amido-4-methylcoumarin, L-Asn-7-amido-4-methylcoumarin, L-Gln-7-amido-4-methylcoumarin, L-Glu-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, L-His-7-amido-4-methylcoumarin, L-Ile-7-amido-4-methylcoumarin, L-Leu-7-amido-4-methylcoumarin, L-Asp-7-amido-4-methylcoumarin, L-Thr-7-amido-4-methylcoumarin, L-Met-7-amido-4-methylcoumarin, L-Trp-7-amido-4-methylcoumarin, L-Ser-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and L-Val-7-amido-4-methylcoumarin
-
-
-
additional information
?
-
no activity with L-Ala-7-amido-4-methylcoumarin, L-Cys-7-amido-4-methylcoumarin, L-Gln-7-amido-4-methylcoumarin, L-Glu-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, L-His-7-amido-4-methylcoumarin, L-Ile-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin, L-Pro-7-amido-4-methylcoumarin, L-Thr-7-amido-4-methylcoumarin, L-Trp-7-amido-4-methylcoumarin, L-Tyr-7-amido-4-methylcoumarin, and L-Val-7-amido-4-methylcoumarin
-
-
-
additional information
?
-
-
no activity with L-alpha-Asn-2-naphthylamide, L-Glu-2-naphthylamide, L-Ile-2-naphthylamide, L-Phe-2-naphthylamide, L-Pro-2-naphthylamide, L-Ser-2-naphthylamide, L-Thr-2-naphthylamide, L-Trp-2-naphthylamide, L-Val-2-naphthylamide, and L-Arg-L-Arg-2-naphthylamide
-
-
-
additional information
?
-
-
no detectable activity with L-Asp-2-naphthylamide
-
-
-
additional information
?
-
Streptococcus gordonii FSS2
proteolysis is restricted to peptides with an arginine residue in the N terminus, with cleavage detected only when a hydrophobic or an uncharged residue occupies the second site, the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Arg-peptides + H2O
?
show the reaction diagram
-
-
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
or Lys-peptides, metabolism of kinin
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
takes part in later stages of protein degradation in chloroplasts
-
-
-
Arg-peptides + H2O
?
show the reaction diagram
-
attribution to inflammatory and wound healing processes
-
-
-
additional information
?
-
Q6P179
the enzyme is induced by interferon-gamma, the enzyme can trim the N-terminal extended precursor to antigenic peptides in the endoplasmic reticulum
-
-
?
additional information
?
-
Q938E9
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
-
?
additional information
?
-
O09175
the enzyme plays a role in peptide or protein precursor processing, the enzyme expression is up-regulated during ontogenesis
-
-
-
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development
-
-
-
additional information
?
-
-
the enzyme probably is involved in the final stages of peptide and protein precursor processing and maturation mechanisms via the exopeptidase pathway and thereby in some inflammatory processes and tumour development, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
-
additional information
?
-
Streptococcus gordonii FSS2
Q938E9
the enzyme may serve as a critical factor for arginine acquisition during nutrient stress in vivo and also in the proteolysis of host proteins and peptides during SBE pathology
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Br-
-
activation
Ca2+
5 mM, activation to 150% of control
Ca2+
-
26% activation at 0.1 mM
Cd2+
-
activates
Cd2+
-
inhibitor
Cl-
-
required for activity
Cl-
-
required for activity
Cl-
-
activates
Cl-
-
activates at physiological concentrations
Cl-
-
activates at physiological concentrations around 150 mM, dependent on the target peptide
Co2+
-
activates. Enzyme contains 0.00063 atoms per subunit, wild-type enzyme
Co2+
-
; the metal-substituted derivative Co(II)-Ap-B contains almost 1 mol of cobalt(II) ions molecule
Co2+
-
0.5 mM enhances activity
Co2+
-
slight enzyme activation
Cu2+
-
; the metal-substituted derivative Cu(II)-Ap-B contains almost 1 mol of copper(II) ions per molecule
Fe2+
-
inhibitor
Fe3+
-
29% activation at 0.1 mM
Hg2+
-
inhibitor
K+
5 mM, activation to 131% of control
K+
-
0.4 M activates the activity by 55%
KCl
-
activation
KCl
-
enhances activity, maximal activation at 50 mM
Li+
-
0.4 M activates the activity by 45%
Mg2+
-
22% activation at 10
Mn2+
-
activates. Enzyme contains 0.0026 atoms per subunit, wild-type enzyme
Na+
200 mM, activation to 166% of control
Na+
-
3fold increase of activity at 0.2 mM
Na+
380% increase of activity at 150 mM
Na+
-
110% increase of activity at 150 mM
Na+
-
0.4 M activates the activity by 190%
NaCl
-
activation
NaCl
-
enhances activity
NaCl
-
absolutely required for activity
NH4Cl
-
enhances activity, maximal activation at 100 mM
Ni2+
-
activates
Ni2+
-
inhibitor
Sn2+
-
slight enzyme activation
Zinc
essential zinc-binding site HEXXH at amino acid residues 370-374 with a second glutamic acid separated by 18 amino acids
Zn2+
-
restores activity after inhibition with 1,10-phenanthroline
Zn2+
-
contains 1 mol per mol of the enzyme
Zn2+
-
enzyme contains 0.036 atoms per subunit, wild-type enzyme
Zn2+
zinc-metalloaminopeptidase, 2 Zn2+ per enzyme molecule
Zn2+
-
zinc-metallopeptidase
Zn2+
-
34% activation at 0.1 mM
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
Zn2+
-
; Ap-B contains 1 mol of Zn2+ ions per molecule
Zn2+
-
metalloenzyme containing Zn2+
Zn2+
-
Zn2+-exopeptidase
Zn2+
-
slight enzyme activation
Mn2+
-
slight enzyme activation
additional information
-
no evidence for Zn in atomic absorption chromatography
additional information
-
metallopeptidase
additional information
-
no activation by metal ions, no metallopeptidase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
activity restored by Co2+
1,10-phenanthroline
effective
1,10-phenanthroline
-
complete inhibition at 1 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
complete inhibition, reversible by Zn2+
1,10-phenanthroline
-
68.5% inhibition at 5 mM
1,10-phenanthroline
-
reversible by Zn2+
1,10-phenanthroline
-
-
1,10-phenanthroline
-
34% residual activity at 1 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1-methyl cyclohexan bestatin
-
i.e. BE15, strong inhibition
2,2'-dipyridyl
-
-
2,4-Dinitrofluorobenzene
-
-
2,6-pyridinedicarboxylate
-
-
2-Chloroethylphosphonic acid
-
-
2-mercaptoethanol
-
enzyme II
2-mercaptoethanol
-
-
3,4-dichloroisocoumarin
-
-
3,4-dichloroisocoumarin
-
0.1 mM, 12% inhibition. 1.0 mM, 16% inhibition
3,4-dichloroisocoumarin
2 mM, 38% inhibition
4-chloromercuribenzoate
-
-
5,5 dithiobis(2-nitrobenzoic acid)
-
1 mM, 74.89% enzyme inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-hydroxyquinoline
-
-
Acetate buffer
-
-
actinonin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
actinonin
-
-
Ag+
-
complete inhibition at 0.1 mM
amastatin
1 mM, 11% inhibition
amastatin
-
amastatin
-
50-70% inhibition at 0.0003 mM, dependent on TGF-beta1 activation
amastatin
-
-
amino acids
-
-
amino acids
-
-
amino acids
-
-
antipain
-
-
Aprotinin
-
34% residual activity at 0.25 mg/ml
apstatin
0.1 mM, 50% inhibition
Arg
-
noncompetitive
Arg
-
competitive
arginine derivatives
-
with carboxyl or alpha-amino group blocked
arphamemine B
-
-
arphamenine
-
aminopeptidase B-specific inhibitor
-
Arphamenine A
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
Arphamenine A
complete inhibition at 0.1 mM
Arphamenine A
-
complete inhibition at 0.1 mM
Arphamenine A
-
-
Arphamenine B
aminopeptidase B-specific inhibitor
Arphamenine B
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
Arphamenine B
-
-
bestatin
-
analogues
bestatin
-
-
bestatin
-
stereoisomers
bestatin
1 mM, 32% inhibition
bestatin
-
strong inhibition
bestatin
orally applicated inhibits the melanoma cell-induced angiogenesis in mice air sacs
bestatin
-
-
bestatin
-
84.8% inhibition at 0.3 mM
bestatin
-
the native enzyme is completely inhibited at 0.05 mM, the recombinant enzyme is completely inhibited at 0.1 mM
bestatin
complete inhibition at 0.1 mM
bestatin
-
complete inhibition at 0.1 mM
bestatin
-
highly sensitive to bestatin
beta-mercaptoethanol
4% inhibition at 10 mM
beta-mercaptoethanol
-
20% inhibition at 10 mM
bipyridine
-
-
Borax-pyruvic acid buffer
-
-
-
Ca2+
-
0.1 mM CaCl2, 19% inhibition
Ca2+
-
16% inhibition at 1 mM, 24% inhibition at 10 mM
Ca2+
-
slight inhibition at 1 mM
Ca2+
-
19% inhibition at 1 mM
Cd2+
-
-
Cd2+
-
-
Cd2+
-
inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme
Cd2+
-
complete inhibition at 1 mM
cementoin
-
-
-
citric acid-sodium citrate buffer
-
-
-
Co2+
-
-
Co2+
-
0.1 mM CoCl2, 23% inhibition
Co2+
-
inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme
Co2+
-
strong inhibition at 1 mM
Co2+
62% inhibition at 1 mM
Co2+
-
45% inhibition at 1 mM
Co2+
-
76% inhibition at 1 mM
Cu2+
-
-
Cu2+
-
-
Cu2+
-
0.1 mM CuCl2, complete inhibition
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
84% inhibition at 0.1 mM
Cu2+
-
complete inhibition at 1 mM
Cyclopeptide OF49-II
-
from Penicillium regulosum, total synthesis
-
cysteine
-
enzyme II
cysteine
21% inhibition at 1 mM
cysteine
-
15% inhibition at 1 mM
D,L-Homolysine
-
-
D-Arg
-
-
D-penicillamine
-
-
DFP
5 mM, 25% inhibition. 10 mM, 44% inhibition
dithiothreitol
-
-
dithiothreitol
33% inhibition at 10 mM
dithiothreitol
-
54% inhibition at 10 mM
DTT
-
25% inhibition at 1 mM, complete inhibition at 10 mM
DTT
-
9% inhibition at 1 mM
DTT
-
1 mM, complete inhibition of enzyme activity
DX600
-
only blocks human ACE2 activity but not mouse
E-64
-
99% residual activity at 0.1 mM
E64
48% inhibition at 0.01 mM
E64
-
12% inhibition at 0.01 mM
EDTA
-
complete loss of activity after dialysis with EDTA
EDTA
-
complete inhibition at 1-10 mM
EDTA
-
90% inhibition at 1 mM
EDTA
-
the native enzyme is inhibited by 95% at 10 mM, the recombinant enzyme is inhibited by 71% at 10 mM
EDTA
12% inhibition at 1 mM
EDTA
-
54% inhibition at 1 mM
EDTA
-
61% residual activity at 1 mM
EDTA
-
1 mM, 42.33% enzyme inhibition
EGTA
-
complete inhibition at 1 mM
ethanol
-
-
ethyliodoacetate
-
-
Fe2+
-
-
Fe2+
-
inhibits the Ni2+-saturated enzyme
Glu-pyrrolidide
0.1 mM, 98% inhibition
glutathione
-
high concentration
Gly-Gly
5 mM, 8% inhibition
Hg2+
-
-
Hg2+
-
-
Hg2+
-
-
Hg2+
-
0.1 mM HgCl2, complete inhibition
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 0.1 mM
Hg2+
-
complete inhibition at 1 mM
HgCl2
-
complete inhibition at 1 mM
iodoacetamide
5 mM, 9% inhibition
iodoacetamide
-
16% inhibition at 1 mM
iodoacetate
-
0.1 mM, complete inactivation
Iodobenzoate
-
-
-
kallidin
-
human peptide hormone, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 73.7% (wild-type enzyme)
L-1-tosylamido-2-phenylethylchloromethylketone
-
-
L-Arg
5 mM, 70% inhibition
L-Arg-2-naphthylamide
-
competitive inhibition of hydrolysis of L-Ala-2-naphthylamide, no inhibition vice versa
L-Lys
5 mM, 28% inhibition
L-Lysinethiol
-
-
L-Penicillamine
-
-
Leucine hydroxamate
-
-
leucinthiol
-
-
leuhistin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
Leupeptin
-
5% inhibition at 0.01 mM
Leupeptin
-
-
Lys
-
noncompetitive
Lys
-
competitive
methyl bestatin
-
-
Mg2+
-
slight inhibition at 1 mM
MgCl2
-
0.1 mM MgCl2, 22% inhibition
MLN-4760
-
MLN-4760 inhibits both human and mouse ACE2
Mn2+
-
complete inhibition at 10 mM
Mn2+
-
strong inhibition at 1 mM
N-alpha-p-Tosyl-L-lysine
-
-
N-alpha-p-tosyl-L-lysine-chloromethyl ketone
-
specific and irreversible inhibitor
N-ethylmaleimide
-
-
N-ethylmaleimide
-
the native enzyme is inhibited by 45% at 1 mM, the recombinant enzyme is inhibited by 71% at 1 mM
N-ethylmaleimide
44% inhibition at 0.1 mM
N-ethylmaleimide
-
21% inhibition at 0.1 mM
N-[(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl]-L-valyl-L-valyl-L-aspartic acid
-
-
N-[1-(R,S)-carboxy-3-phenyl propyl] Ala-Ala-Phe-p-aminobenzoate
-
-
Na+
-
NaCl (0.1-100 mM) has an opposite effect on the EGTA-treated KAP apo-enzyme, it inhibits 13% at 0.1 mM and 100% at 100 mM
NaI
-
-
NEM
-
13% inhibition at 1 mM
Ni2+
-
-
Ni2+
-
inhibits Cd2+-saturated enzyme
Ni2+
-
strong inhibition at 1 mM
Ni2+
75% inhibition at 1 mM
Ni2+
-
63% inhibition at 1 mM
Ni2+
-
complete inhibition at 1 mM
nitrobestatin
-
92.3% inhibition at 0.133 mM
o-phenanthroline
-
the native enzyme is inhibited by 76% at 0.5 mM, the recombinant enzyme is inhibited by 80% at 0.5 mM
p-aminophenylmercuric acetate
-
1 mM, 41.27% enzyme inhibition
p-chloromercuribenzene sulfonic acid
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuriphenyl sulfonic acid
-
1 mM, 72.22% enzyme inhibition
p-Hydroxymercuriphenylsulfonic acid
-
-
Pb2+
-
-
Pb2+
-
84% inhibition at 1 mM
PCMB
2 mM, complete inactivation
pefabloc
5 mM, 60% inhibition. 10 mM 69% inhibition
pefabloc
-
-
Pepstatin
-
5% inhibition at 0.01 mM
Pepstatin
-
93% residual activity at 0.1 mM
Phe
-
noncompetitive
Phenylmethanesulfonylfluoride
10% inhibition at 0.1 mM
Phenylmethanesulfonylfluoride
-
1% inhibition at 0.1 mM
Phenylmethanesulfonylfluoride
-
45% residual activity at 0.5 mM
phosphate
-
-
PMSF
-
14% inhibition at 1 mM
Porphyrindine
-
-
pre-elafin
-
-
-
puromycin
weak
puromycin
10% inhibition at 0.1 mM
puromycin
-
1% inhibition at 0.1 mM
SDS
5%, 96% inhibition
Substance P
-
human peptide hormone, 100 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 63.8% (wild-type enzyme); human peptide hormone, 10 microM, Arg 4-methylcoumarin 7-amide hydrolysis: 78% (wild-type enzyme)
tert-butyl bestatin
-
i.e. BE17, the BE15 derivative has a dual inhibitory effect of invasion and motility on tumor and endothelial cells
thioglycolic acid
-
-
Urea
2 M, 18% inhibition
Zn2+
-
-
Zn2+
-
at 0.5 mM
Zn2+
-
0.1 mM ZnCl2, 82% inhibition
Zn2+
-
inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme
Zn2+
-
complete inhibition at 0.1-10 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
complete inhibition at 0.1 mM
Zn2+
-
99% inhibition at 0.1 mM
Zn2+
-
80% inhibition at 1 mM
Zn2+
-
Zn2+ inhibits AP-B reversibly at micromolar concentrations (0.005-0.05 mM), AP-B with 0.25 Zn2+ becomes susceptible to degradation by trypsin suggesting that Zn2+ alters enzyme conformation, complete inhibition occurs at 0.050-0.080 mM
ZnCl2
-
96% inhibition at 1 mM
ZnCl2
-
-
Mn2+
-
82% inhibition at 1 mM
additional information
EDTA has no effect up to 1 mM
-
additional information
-
inhibitory potency of bestatin and derivatives on enzyme activity, umbilical vein endothelial cell vessel formation, and cell invasion and migration, overview
-
additional information
-
no or poor inhibition of L-Arg-2-naphthylamide hydrolysis by puromycin at 1 mM, aprotinin, pepstatin A, E64, chymostatin, imipramine, phosphoramidon, lisinopril, and apstatin
-
additional information
-
no inhibition by phosphoramidon, E64, antipaine, and TLCK
-
additional information
-
no inhibition by pepstatin
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
additional information
-
no inhibition at 0.1 mM by Mg2+
-
additional information
-
no inhibition by puromycin
-
additional information
-
no inhibition by PMSF, pepstatin, and aprotinin
-
additional information
-
not affected by phenylmethylsulfonylfluoride
-
additional information
-
insensitive to L-Arg-hydroxamate, L-Lys-hydroxamate, puromycin, and amastatin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
2-mercaptoethanol
1 mM, activation to 160% of control
acetate
-
activation
bacitracin
-
activation
cysteine
-
slight activation
diphosphate
-
activation in presence of low Cl- concentrations
dithiothreitol
-
activation, enzyme II
dithiothreitol
-
activation
dithiothreitol
-
activation
E64
-
slight activation at 0.01-0.05 mM
EDTA
-
activation
EDTA
-
0.1 mM, activation to 128% of control. 1.0 mM, activation to 146% of control
EDTA
5 mM, activation to 131% of control
L-Cys
5 mM, activation to 148% of control
NaF
-
0.4 M activates the activity by 20%
phosphate
-
activation
sulfhydryl compounds
-
activation, enzyme I
TGF-beta1
-
activates aminopeptidase activity
-
Zn2+
-
low levels of Zn2+ at 0.00025-0.002 mM result in some activation of AP-B activity up to 25-40% above controls (without Zn2+)
additional information
-
the enzyme is cold-active
-
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0533
Arg 4-methylcoumarin 7-amide
-
pH 7.4, 37C, wild-type
0.0774
Arg 4-methylcoumarin 7-amide
-
pH 7.4, 37C, mutant Q169N
0.00318
Arg-4-methylcoumaryl-7-amide
pH 7.5, 37C
0.051
Arg-4-nitroanilide
pH 7.8, 37C
0.0159
Arg-7-amido-4-methylcoumarin
-
pH 5.0, 37C
0.014
Arg-alpha-atrial natriuretic factor1-20
-
-
-
0.183
Arg-beta-naphthylamide
-
Co(II)-Ap-B
0.267
Arg-beta-naphthylamide
-
Ap-B
0.111
Arg-Leu-enkephalin
-
-
0.005
Arg-Lys-somatostatin-14
-
-
0.021
Arg-Met-enkephalin
-
pH 7.4, 37C, wild-type
0.111
Arg-Met-enkephalin
-
pH 7.4, 37C, mutant Q169N
0.125
Arg-Met-enkephalin
-
-
0.058
Arg-neurokinin A
-
-
0.07
arginyl-4-methylcoumarin 7-amide
-
enzyme I
0.27
arginyl-4-methylcoumarin 7-amide
-
enzyme II
7.8
Cys-Gly
-
pH 7.5, 37C
0.0157
kallidin
-
pH 7.4, 37C, wild-type
0.0651
kallidin
-
pH 7.4, 37C, mutant Q169N
10
L-Ala-4-nitroanilide
pH 8.0, 30C
0.043
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, -1C
0.058
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, 9C
0.072
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, 19C
0.00003
L-Arg-2-naphthylamide
-
mutant enzyme D406N
0.000062
L-Arg-2-naphthylamide
-
mutant enzyme E26oQ
0.000064
L-Arg-2-naphthylamide
-
mutant enzyme E268Q
0.000088
L-Arg-2-naphthylamide
-
wild type enzyme
0.000099
L-Arg-2-naphthylamide
-
mutant enzyme E256Q
0.000105
L-Arg-2-naphthylamide
-
mutant enzyme D405E
0.000109
L-Arg-2-naphthylamide
-
mutant enzyme E387Q
0.000111
L-Arg-2-naphthylamide
-
mutant enzyme E388Q
0.000119
L-Arg-2-naphthylamide
-
mutant enzyme E267Q
0.000123
L-Arg-2-naphthylamide
-
mutant enzyme D405N
0.000125
L-Arg-2-naphthylamide
-
mutant enzyme D315N
0.000128
L-Arg-2-naphthylamide
-
mutant enzyme E410Q
0.000183
L-Arg-2-naphthylamide
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25C
0.000267
L-Arg-2-naphthylamide
-
recombinant Ap-B, at pH 7.4 and 25C
0.000384
L-Arg-2-naphthylamide
-
mutant enzyme E414Q
0.000578
L-Arg-2-naphthylamide
-
mutant enzyme D405A
0.02
L-Arg-2-naphthylamide
-
-
0.0453
L-Arg-2-naphthylamide
-
pH 7.4, 37C, mutant Y441F
0.06
L-Arg-2-naphthylamide
-
pH 7.4, 37C, mutant Y229H
0.0987
L-Arg-2-naphthylamide
-
pH 7.4, 37C, mutant Y409F
0.108
L-Arg-2-naphthylamide
-
-
0.162
L-Arg-2-naphthylamide
-
pH 7.4, 37C, wild-type
0.6
L-Arg-4-nitroanilide
pH 8.0, 30C
0.048
L-Arg-7-amido-4-methylcoumarin
-
-
0.091
L-Arg-7-amido-4-methylcoumarin
-
0.0026
L-Arg-beta-naphthylamide
-
enzyme I
0.02
L-Arg-beta-naphthylamide
-
-
0.038
L-Arg-beta-naphthylamide
-
enzyme II
0.3
L-Arg-beta-naphthylamide
-
-
3.6
L-Leu-4-nitroanilide
pH 8.0, 30C
0.00014
L-Lys-2-naphthylamide
-
wild type enzyme
0.000213
L-Lys-2-naphthylamide
-
mutant enzyme D405E
0.0169
L-Lys-2-naphthylamide
-
mutant enzyme D405A
0.036
L-Lys-2-naphthylamide
-
-
0.135
L-Lys-2-naphthylamide
-
-
0.333
L-Lys-2-naphthylamide
-
-
0.0544
L-Lys-4-nitroanilide
-
pH 7.5, 37C
0.85
L-Lys-4-nitroanilide
pH 8.0, 30C
0.12
L-Lys-beta-naphthylamide
-
-
0.36
L-Lys-beta-naphthylamide
-
-
1.2
L-Lys-p-nitroanilide
-
-
0.000124
L-Tyr-2-naphthylamide
-
mutant enzyme D405A
0.000197
L-Tyr-2-naphthylamide
-
wild type enzyme
19
L-Val-4-nitroanilide
pH 8.0, 30C
4.9
Leu-4-nitroanilide
-
pH 7.5, 37C
13.5
Leu-Gly
-
pH 7.5, 37C
0.381
Lys 4-methylcoumarin 7-amide
-
pH 7.4, 37C, wild-type
-
0.568
Lys 4-methylcoumarin 7-amide
-
pH 7.4, 37C, mutant Q169N
-
0.026
Lys-7-amido-4-methylcoumarin
-
pH 5.0, 37C
0.28
lysyl-4-methylcoumarin 7-amide
-
enzyme I
0.4
lysyl-4-methylcoumarin 7-amide
-
enzyme II
0.0251
Met-enkephalin
-
pH 7.4, 37C, wild-type
0.1
N-naphthalen-2-yl-L-argininamide
-
free enzyme
0.1
N-naphthalen-2-yl-L-argininamide
-
-
0.2
N-naphthalen-2-yl-L-argininamide
-
immobilized enzyme
0.36
Met-enkephalin
-
pH 7.4, 37C, mutant Q169N
additional information
additional information
-
comparison of values for various peptide substrates and enzyme sources
-
additional information
additional information
-
dependency on chloride concentration
-
additional information
additional information
-
dependency on chloride concentration; dependency on pH and temperature
-
additional information
additional information
-
-
-
additional information
additional information
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.06
Arg 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
9.27
Arg 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, wild-type
2.3
Arg-4-methylcoumaryl-7-amide
Homo sapiens
Q6P179
pH 7.5, 37C
53.1
Arg-beta-naphthylamide
Rattus norvegicus
-
Ap-B
69.5
Arg-beta-naphthylamide
Rattus norvegicus
-
Co(II)-Ap-B
1.07
Arg-Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
3.63
Arg-Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, wild-type
10700
Cys-Gly
Escherichia coli
-
pH 7.5, 37C
1.99
kallidin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
2.35
kallidin
Homo sapiens
-
pH 7.4, 37C, wild-type
0.37
L-Ala-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30C
0.043
L-Ala-Ala-Pro-Leu-4-nitroanilide
Colwellia psychrerythraea
-
pH 7.2, -1C
0.13
L-Ala-Ala-Pro-Leu-4-nitroanilide
Colwellia psychrerythraea
-
pH 7.2, 9C
0.36
L-Ala-Ala-Pro-Leu-4-nitroanilide
Colwellia psychrerythraea
-
pH 7.2, 19C
0.49
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405A
2.1
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405N
2.3
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y441F
4.8
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y409F
6.3
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E410Q
9.4
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y229H
11.5
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405E
11.7
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E268Q
12
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E26oQ
13.5
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E414Q
19.6
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D406N
20
L-Arg-2-naphthylamide
Rattus norvegicus
-
-
24.1
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E267Q
25
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, wild-type
38
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D315N
51.8
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E256Q
53.1
L-Arg-2-naphthylamide
Rattus norvegicus
-
recombinant Ap-B, at pH 7.4 and 25C
53.3
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E388Q
54.1
L-Arg-2-naphthylamide
Rattus norvegicus
-
wild type enzyme
60
L-Arg-2-naphthylamide
Rattus norvegicus
-
mutant enzyme E387Q
69.47
L-Arg-2-naphthylamide
Rattus norvegicus
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25C
34
L-Arg-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30C
55
L-Leu-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30C
0.037 - 0.23
L-Lys-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405E
0.83
L-Lys-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405A
3
L-Lys-2-naphthylamide
Rattus norvegicus
-
-
23.6
L-Lys-2-naphthylamide
Rattus norvegicus
-
wild type enzyme
79.3
L-Lys-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405E
10
L-Lys-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30C
1
L-Tyr-2-naphthylamide
Rattus norvegicus
-
mutant enzyme D405A
2.1
L-Tyr-2-naphthylamide
Rattus norvegicus
-
wild type enzyme
0.43
L-Val-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30C
307
Leu-4-nitroanilide
Escherichia coli
-
pH 7.5, 37C
6630
Leu-Gly
Escherichia coli
-
pH 7.5, 37C
1.95
Lys 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
-
14.9
Lys 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, wild-type
-
0.47
Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, wild-type
0.48
Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
52400
Arg 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
43784
175000
Arg 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, wild-type
43784
10.4
Arg-Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
59231
173
Arg-Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, wild-type
59231
30.1
kallidin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
3696
156
kallidin
Homo sapiens
-
pH 7.4, 37C, wild-type
3696
48
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y409F
1887
51
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y441F
1887
154
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, wild-type
1887
157
L-Arg-2-naphthylamide
Rattus norvegicus
-
pH 7.4, 37C, mutant Y229H
1887
3440
Lys 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
202260
39200
Lys 4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.4, 37C, wild-type
202260
1
Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
2567
19
Met-enkephalin
Homo sapiens
-
pH 7.4, 37C, wild-type
2567
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
1,10-phenanthroline
-
-
0.02
actinonin
-
at 37C in Bicine buffer complemented with 0.2 M NaCl
0.0125
arphamemine B
-
at 37C in Bicine buffer complemented with 0.2 M NaCl
0.0000076
Arphamenine A
-
pH 7.4, 37C, mutant Y229H
0.0000085
Arphamenine A
-
pH 7.4, 37C, wild-type
0.0000085
Arphamenine B
-
pH 7.4, 37C, mutant Y229H
0.0000103
Arphamenine B
-
pH 7.4, 37C, wild-type
0.00021
bestatin
-
at 37C in Bicine buffer complemented with 0.2 M NaCl
0.024
Leucine hydroxamate
-
at 37C in Bicine buffer complemented with 0.2 M NaCl
0.006
Zn2+
-
in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, at 37C
0.00054
leucinthiol
-
at 37C in Bicine buffer complemented with 0.2 M NaCl
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006
1,10-phenanthroline
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
0.000077
1,10-phenanthroline
Homo sapiens
-
pH 7.4, 37C, wild-type
0.00000316
Arphamenine A
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
0.00000373
Arphamenine A
Homo sapiens
-
pH 7.4, 37C, wild-type
0.00000072
Arphamenine B
Homo sapiens
-
pH 7.4, 37C, wild-type
0.00000155
Arphamenine B
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
0.00000349
bestatin
Homo sapiens
-
pH 7.4, 37C, wild-type
0.000289
bestatin
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
0.00000391
ZnCl2
Homo sapiens
-
pH 7.4, 37C, wild-type
0.00000592
ZnCl2
Homo sapiens
-
pH 7.4, 37C, mutant Q169N
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00011
-
plasma enzyme, 37C
0.00012
-
plasma enzyme, 20C
0.0003
-
plasma enzyme, 20C
0.00031
-
plasma enzyme, 20C
0.00082
-
plasma enzyme, 37C
0.0011
-
plasma enzyme, 37C
0.0016
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of adrenal gland
0.0018
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of lung
0.002
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of heart
0.0024
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of kidney cortex
0.0042
-
normal healthy rats and rats treated/deprived with salt and water, soluble fraction of kidney medulla
0.06708
-
after purification
0.1
-
Cu(II)-Ap-B; metal-substituted enzyme form Cu(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25C
0.63
-
purified enzyme
2.16
-
-
9.9
-
-
9.9
-
Co(II)-Ap-B; metal-substituted enzyme form Co(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25C
12.5
-
Ap-B; recombinant Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25C
26
-
-
26
-
purified enzyme, substrate N-succinyl-Gly-Pro-Leu-Gly-Pro 7-amido-4-methylcoumarin
55
-
purified enzyme, substrate L-Leu 7-amido-4-methylcoumarin
64
purified recombinant enzyme
140
-
purified enzyme, substrate L-Tyr 7-amido-4-methylcoumarin
263.7
-
purified enzyme, substrate L-Arg 7-amido-4-methylcoumarin
297.9
-
purified enzyme
6974
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
-
5.5 - 6.5
-
-
6.5
-
assay at
7.2
-
presence of 0.2 M added Cl-
7.2
-
assay at
7.4
-
free enyzme
7.4
-
assay at
7.5
-
without added Cl-
7.5
-
-
7.5
-
activity assay
7.8
-
immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
-
pH 4.5: about 80% of maximal activity, pH 5.5: about 25% of maximal activity, activity is negligible at pH values beyond pH 4.0 and pH 6.0
5.5 - 8.25
-
-
6 - 9
-
pH profile
7 - 9
-
narrow pH-optimum
7.5 - 9.5
-
-
additional information
-
broad activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
activity assay
28 - 32
-
-
37
-
in vivo assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
45
-
free enzyme
50
-
immobilized enzyme
additional information
-
the enzyme is cold-active
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
-
15C: about 30% of maximal activity, 25C: about 75% of maximal activity, 45C: about 70% of maximal activity
20 - 37
-
higher activity at 20C
20 - 37
-
higher activity at 37C
35 - 80
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
-
chromatofocusing
4.9
-
experimental
5.1
-
isoelectric focusing
5.3
calculated from amino acid sequence
5.6 - 5.9
isoelectric focusing
5.83
-
theoretical
7.5
-
band I, isoelectric fosusing
8.8
-
band II, isoelectric fosusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
cortex and anterior brain, striatum and middle brain, posterior brain
Manually annotated by BRENDA team
-
highest enzyme activity
Manually annotated by BRENDA team
-
colorectal adenocarcinoma cell line
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
cardiac, ventricular
Manually annotated by BRENDA team
-
pituitary tumor-derived cell line
Manually annotated by BRENDA team
-
cardiac ventricular fibroblastic cell
Manually annotated by BRENDA team
-
neutrophilic promyelocyte cell line
Manually annotated by BRENDA team
-
T-lymphoma cell line
Manually annotated by BRENDA team
-
lymphoma cell line
Manually annotated by BRENDA team
-
chronic myeloid leukemia cell line
Manually annotated by BRENDA team
-
cortex and medulla
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
peripheral, high enzyme activity
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
highest enzyme activity
Manually annotated by BRENDA team
-
adrenal pheochromocytoma cell line
Manually annotated by BRENDA team
-
enzyme probably derived from blood
Manually annotated by BRENDA team
-
intermediate lobe
Manually annotated by BRENDA team
-
primary pituitary gland cell line
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
lymphoblast-like cell line
Manually annotated by BRENDA team
enzyme expression from embryo to adult rat, neuronal cell, developmental distribution, overview
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
ocurrence of enzyme dependent on development of spermatides
Manually annotated by BRENDA team
involvement in secretory pathway
Manually annotated by BRENDA team
-
highest enzyme activity, mainly expressed in late spermatids during maturation
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
additional information
developmental expression and activity pattern of Ap-B, in-situ hydridization, overview
Manually annotated by BRENDA team
additional information
-
the enzyme is up-regulated during long-term activation of normal and lymphoma T-cells
Manually annotated by BRENDA team
additional information
-
tissue distribution of enzyme activity, overview
Manually annotated by BRENDA team
additional information
-
ubiquitous tissue distribution, expression level is tissue- and cell-type-dependent
Manually annotated by BRENDA team
additional information
-
wide tissue distribution, expression level is tissue- and cell-type-dependent
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of germinal cells, proacrosmic granule of round spermatids
-
Manually annotated by BRENDA team
-
of late spermatids
Manually annotated by BRENDA team
Streptococcus sanguinis 903
-
-
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted, in PC-12 cells the active enzyme is associated to the external surface of the plassma mamabrane
-
Manually annotated by BRENDA team
Streptococcus gordonii FSS2
-
-
-
-
Manually annotated by BRENDA team
-
or loosly associated with cytoplasmic membrane, enzyme II
-
Manually annotated by BRENDA team
-
from pituitary gland, associated to membrane
-
Manually annotated by BRENDA team
-
from Jurkat lymphocytes
-
Manually annotated by BRENDA team
-
synaptic-like vesicles in brain
-
Manually annotated by BRENDA team
present in secretory vesicles that contain cathepsin L with the neuropeptides enkephalin and neuropeptide Y
-
Manually annotated by BRENDA team
-
present in secretory vesicles that contain cathepsin L with the neuropeptides enkephalin and neuropeptide Y
-
Manually annotated by BRENDA team
-
synaptic membrane
Manually annotated by BRENDA team
additional information
-
subcellular localization, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000 - 58000
-
gel filtration, comparison with enzyme from other sources
35976
52000 - 58000
-
gel filtration, enzyme I
35979
52000 - 58000
-
gel filtration
35984
62000
-
gel filtration
682114
64000
gel filtration
651488
71000
-
gel filtration
663693
72000
-
SDS-PAGE
678924
72000 - 75000
-
gel filtration
35970
72000 - 75000
-
SDS-PAGE, HPLC
35973
72000 - 75000
-
gel filtration
35978
72000 - 75000
-
gel filtration
36000
72000 - 75000
-
-
36004
72000 - 75000
-
gel filtration
36004
72000 - 75000
-
non-denaturing PAGE
36005
72000 - 75000
-
gel filtration
36006
72100
calculated from amino acid sequence
681522
72550
-
deduced from amino acid sequence
678144
73000
SDS-PAGE
731085
74000
SDS-PAGE
681522
74000
-
SDS-PAGE
681522
74000
-
in the absence of ZnCl2, SDS-PAGE, after incubation with trypsin
697931
78000
-
native PAGE
666143
79700
-
SDS-PAGE
710446
80200
-
Sephadex G-200
710446
95000
-
gel filtration
35991, 35996
97400
-
SDS-PAGE
707346
105000
-
gel filtration
35983
110000
-
gel filtration
664982
180000
-
gel filtration
649371
220000
-
gel filtration
36007
270000
-
gel filtration
666520
360000
-
gel filtration, enzyme II
35979
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 110000, reducing SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
monomer
-
1 * ?, enzyme I, SDS-PAGE
monomer
-
-
monomer
-
1 * 73000, SDS-PAGE
monomer
1 * 70000, SDS-PAGE
monomer
-
1 * 71000, SDS-PAGE
monomer
-
1 * 95500, liver enzyme, 1 * 72300, testis enzyme
monomer
-
1 * 72000, testis enzyme
monomer
-
1 * 72000, SDS-PAGE
monomer
-
-
monomer
Streptococcus gordonii FSS2
-
1 * 70000, SDS-PAGE
-
oligomer
-
x * 86000, SDS-PAGE
polymer
-
? * 83000, SDS-PAGE
tetramer
-
4 * 25500, SDS-PAGE after treatment with mercaptoethanol
trimer
-
3 * 60000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
-
-
glycoprotein
contains high mannose-type sugar chains
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized using the hanging-drop vapour diffusion method. X-ray diffraction data to 2.3 A resolution are collected using an orthorhombic crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.55, b = 130.86, c = 170.87 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
free enzyme
707346
6 - 9
-
-
710446
6 - 9.5
-
immobilized enzyme
707346
6.6 - 7
-
stable
666520
7 - 9
-
purified enzyme, 4C, 12 h, stable
664982
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-20
-
inactivation
35984
4
24 h, minimally affected
651488
20
-
30 min, completely stable
664867
25
-
best stability
35984
25
unstable after 24 h
651488
30
-
half-life is 67 min
663693
37
-
pH 5.1-5.5, several hours
35996
37
unstable after 24 h
651488
40
-
inactivation above
35991
40
-
half-life is 38 min
663693
40
-
30 min, 95% activity remaining
664867
45
-
half-life is 10 min
663693
47
-
pH 6.5-8.1, 30 min
35996
50
-
inactivation
35984
50
-
half-life is 5 min
663693
50
-
10 min, complete loss of activity
666520
50 - 88
-
1 h, loss of activity
664982
51
-
fast inactivation with 0.2 M added Cl-, slow inactivation without added Cl-
35983
52
-
pH 7.0, slow inactivation
35996
55
-
EDTA-dialyzed enzyme is completely inactivated within 2 min. The enzyme of which the divalent cation has has been replaced with Mn2+ or Co2+ is quite stable up to 10 min. The Mn2+-dialyzed sample gradually loses its activity, only 75% of its original levels remains after 10 min
650625
55
-
30 min, 50% activity remaining
664867
60
-
complete inactivation
35998
60
-
30 min, residual activity remaining
664867
60
-
immobilized enzyme with 55% remaining enzyme activity at 60C, free enzyme with 45% remaining activity at 60C
707346
80
20 min, purified recombinant enzyme, stable
664989
additional information
-
stabilized against heat in the presence of Mn2+ or Co2+
650625
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing inactivates
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
-
immobilized enzyme stable at higher concentrations compared to free enzyme
Ethanol
-
15%, immobilized enzyme still 58% remaining activity, free enzyme inactivated
urea
-
at 1.5 M urea only 10% remaining enzyme acitvity, at 2.0 M urea complete loss of enzyme activity
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
methylene blue plus light causes photooxidation
-
35994
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or 4C, 10 d, 100% activity, 30 d 25% acitvity
-
4C, 0.01 M beta,beta-dimethylglutarate buffer, pH 7.2, 0.1 mM DTT
-
6C, 6 d
-
0-4C, citric acid-phosphate buffer or Tris-HCl buffer, 30 days, increase of activity
-
4C, 0.01 M beta,beta-dimethylglutarate buffer, pH 7.2, 0.1 mM DTT
-
4C, pH 6.0, 3.5% (NH4)2SO4, aggregation of monomers to polymer during storage, decomposition to monomer by substrate
-
-20C, complete inactivation after 2 months
-20C, 40% v/v glycerol, 3-6 months, 80-90% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 5fold from Escherichia coli by ion exchange chromatography
native enzyme 159000fold by ammonium sulfate fractionation, ultrafiltration, cation exchange chromatography and gel filtration
-
279.5fold after heat inactivation, ammonium sulfate fractionation and column chromatographies
-
native enzyme 460fold to homogeneity by ion exchange and hydroxy apatite chromatography, and ion exchange chromatography
-
2 forms
-
expressed in Escherichia coli
-
glutathione-Sepharose 4B column chromatography and Q-Sepharose column chromatography; using a glutathione-Sepharose 4B column, cleaving of the fusion-enzyme by thrombin, using a benzamidine-Sepharose and a Q-Sepharose column
-
glutathione-Sepharose 4B column chromatography and Sephadex G-150 gel filtration
-
native enzyme from testis
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography and DEAE Trisacryl Plus M column chromatography
-
partially, subcellular fractionation
-
Toyopearl DEAE-650 column chromatography, Mono Q column chromatography, and DEAE-650 column chromatography
-
80.9fold to homogeneity by gel filtration, anion exchange chromatography, and again gel filtration
-
native enzyme 69.3fold by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration to homogeneity
-
partially, preparation of spores and subcellular fractionation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ywad, overexpression in Escherichia coli
expressed in Escherichia coli
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
expression in HeLa S3 cells
gene rnpep, DNA and amino acid sequence determination and analysis, localization on chromosome 1q32 in a high transcript density region, genetic organization and structure, overview
-
DNA and amino acid sequence determination and analysis, the gene encoding the enzyme is localized on chromosome 1, genetic organization and structure, overview
-
expressed in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli strain BL21; into the pGEX-4T-3 vector for expression in Escherichia coli BL21 cells
-
expression in Escherichia coli
-
testis enzyme, DNA and amino acid sequence determination and analysis, genetic organization and structure, overview, expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q169E
-
mutant shows no activity
Q169N
-
mutant shows a significant decrease in hydrolytic activity toward the fluorescent substrate Lys-4-methylcoumaryl-7-amide (MCA). Mutant shows an increase in IC50 values of inhibitors that interact with the catalytic pocket of aminopeptidase B. Km (Arg 4-methylcoumarin 7-amide) similar to wild-type, kcat (Arg 4-methylcoumarin 7-amide) decreased compared to wild-type. Km (Lys 4-methylcoumarin 7-amide) increased compared to wild-type, kcat (Lys 4-methylcoumarin 7-amide) decreased compared to wild-type
D315N
-
decreased activity compared to the wild type enzyme
D405N
-
decreased activity compared to the wild type enzyme
D406N
-
decreased activity compared to the wild type enzyme
E256Q
-
decreased activity compared to the wild type enzyme
E260Q
-
decreased activity compared to the wild type enzyme
E267Q
-
decreased activity compared to the wild type enzyme
E268Q
-
decreased activity compared to the wild type enzyme
E300Q
-
no activity
E326A
-
inactive
E326D
-
inactive
E326H
-
inactive
E326Q
-
inactive
E348A
-
inactive
E348D
-
inactive
E348E
-
inactive
E348H
-
inactive
E348Q
-
inactive
E387Q
-
increased activity compared to the wild type enzyme
E388Q
-
decreased activity compared to the wild type enzyme
E410Q
-
decreased activity compared to the wild type enzyme
E414Q
-
decreased activity compared to the wild type enzyme
H325A
-
inactive
H325F
-
inactive
H325Y
-
inactive
H329A
-
inactive
H329F
-
inactive
H329Y
-
inactive
Y229H
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y409F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y441F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
additional information
-
immobilization of enzyme with 1% CaCl2 and 2.5% alginate, increase of in stability for immobilized enzyme