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Information on EC 3.4.11.6 - aminopeptidase B and Organism(s) Rattus norvegicus and UniProt Accession O09175
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3.4.11.6 aminopeptidase BSpecify your search results
Word Map
- 3.4.11.6
- brevis
-
pollicis
-
abductor
-
transcranial
- retina
- 2-amino-4-phosphonobutyrate
-
minimi
-
digiti
-
latency
- bestatin
-
thumb
-
corticospinal
- erg
-
interosseous
-
cmaps
-
intracortical
-
voluntary
-
wrist
-
thenar
- tibialis
-
ulnar
-
electroretinogram
-
motor-evoked
-
flexor
-
radialis
-
interstimulus
-
off-center
-
f-waves
-
antiphase
-
amacrine
-
dark-adapted
-
biceps
-
paired-pulse
- beta-naphthylamide
-
alt-associated
-
carpi
-
brachii
-
anoxygenic
-
electromyographic
- quisqualate
-
photopic
- amastatin
-
short-latency
- drug development
-
3.4.11.1
-
interhemispheric
- alpha-fucosidase
-
hallucis
-
light-evoked
-
puromycin-sensitive
-
imagery
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Synonyms
apb, arylamidase, aminopeptidase b, arginine aminopeptidase, cytosol aminopeptidase, arginyl aminopeptidase, aminopeptidase-b, l-rap, dap bii, arginine-aminopeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, arginine
-
-
-
-
arginine aminopeptidase
arginyl aminopeptidase
arylamidase II
-
-
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
cytosol aminopeptidase
-
-
-
-
L-arginine aminopeptidase
-
-
-
-
additional information
arginine aminopeptidase
-
-
-
-
arginyl aminopeptidase
-
-
-
-
additional information
-
the enzyme belongs to the M1 peptidase family, and is distinct from the leukotriene A4 hydrolase, bleomycin hydrolase, and puromycin-sensitive aminopeptidase
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
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
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
-
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9073-92-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-alpha-atrial natriuretic factor1-20 + H2O
Arg + alpha-atrial natriuretic factor1-20
-
-
-
-
?
Arg-beta-atrial natriuretic factor1-20 + H2O
Arg + beta-atrial natriuretic factor1-20
-
-
-
-
?
Arg-beta-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
substrate used in the activity assay
-
-
?
Arg-Lys-somatostatin-14 + 2 H2O
Arg + Lys + somatostatin-14
-
sequential removal of basic N-terminal residues
-
-
?
Gly-L-Pro-2-naphthylamide + H2O
Gly-L-Pro + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Arg-L-Tyr-Gly-Gly-L-Phe-L-Leu + H2O
L-Arg + L-Tyr-Gly-Gly-L-Phe-L-Leu
-
-
-
-
?
L-Arg-peptide + H2O
L-Arg + peptide
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptides
-
-
?
L-beta-Asn-2-naphthylamide + H2O
L-beta-Asn + 2-naphthylamine
-
9% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Cys-2-naphthylamide + H2O
L-Cys + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
5% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Gly-L-Arg-2-naphthylamide + H2O
L-Gly-L-Arg + 2-naphthylamine
-
250% activity compared to L-Lys-2-naphthylamide
-
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
-
15% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
31% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
-
17% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Lys-L-Ala-2-naphthylamide + H2O
L-Lys-L-Ala + 2-naphthylamine
-
7% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Lys-peptide + H2O
L-Lys + peptide
-
specific for N-terminal Arg or Lys residues, di-, tri-, and polypeptide
-
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
-
2% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
-
0.171% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
2% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
-
7% activity compared to L-Arg-7-amido-4-methylcoumarin
-
-
?
L-Val-2-naphthylamide + H2O
L-Val + 2-naphthylamine
-
0.034% activity compared to L-Arg-2-naphthylamide
-
-
?
leukotriene A4 + H2O
L-Arg + leukotriene B4
-
weak in vitro activity
-
-
?
leukotriene A4 + H2O
leukotriene B4 + ?
-
has a residual catalytic ability to hydrolyze leukotriene A4
-
-
?
Lys-2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
1% activity compared to L-Lys-2-naphthylamide
-
-
?
Gly-2-naphthylamide + H2O
Gly + 2-naphthylamine
-
less than 0.02% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
0.1% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
83% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
17% activity compared to L-Lys-2-naphthylamide
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
41% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
0.171% activity compared to L-Arg-2-naphthylamide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
62% activity compared to L-Lys-2-naphthylamide
-
-
?
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 catalyzes the N-terminal cleavage of basic residues of peptide or protein substrates
-
-
?
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
?
-
-
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
?
-
-
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 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-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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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, the enzyme from testis preferably removes Arg and/or Lys residues from the N-terminus of various peptides
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
Co2+
Cu2+
Na+
Zn2+
additional information
-
no evidence for Zn in atomic absorption chromatography
Cl-
-
activates at physiological concentrations around 150 mM, dependent on the target peptide
Co2+
-
the metal-substituted derivative Co(II)-Ap-B contains almost 1 mol of cobalt(II) ions molecule
Cu2+
-
the metal-substituted derivative Cu(II)-Ap-B contains almost 1 mol of copper(II) ions per molecule
Zn2+
-
dependent on, zinc-metallopeptidase, the enzyme contains the binding motif HEXXHX18E
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bestatin
orally applicated inhibits the melanoma cell-induced angiogenesis in mice air sacs
L-Arg-2-naphthylamide
-
competitive inhibition of hydrolysis of L-Ala-2-naphthylamide, no inhibition vice versa
leuhistin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
N-[(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl]-L-valyl-L-valyl-L-aspartic acid
-
-
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
o-phenanthroline
-
the native enzyme is inhibited by 76% at 0.5 mM, the recombinant enzyme is inhibited by 80% at 0.5 mM
actinonin
-
40% inhibition at 0.0003 mM, independent on TGF-beta1 activation
amastatin
-
50-70% inhibition at 0.0003 mM, dependent on TGF-beta1 activation
arphamenine A
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
Arphamenine B
-
the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM
bestatin
-
the native enzyme is completely inhibited at 0.05 mM, the recombinant enzyme is completely inhibited at 0.1 mM
EDTA
-
the native enzyme is inhibited by 95% at 10 mM, the recombinant enzyme is inhibited by 71% at 10 mM
N-ethylmaleimide
-
the native enzyme is inhibited by 45% at 1 mM, the recombinant enzyme is inhibited by 71% 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
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
-
insensitive to L-Arg-hydroxamate, L-Lys-hydroxamate, puromycin, and amastatin
-
additional information
-
At 0.2 mM, no significant inhibitory effect is observed with caffeic, chlorogenic, ferulic, salicylic and sinapic acids as well as with resveratrol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000183
L-Arg-2-naphthylamide
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25°C
additional information
additional information
-
dependency on pH and temperature
-
additional information
additional information
-
dependency on chloride concentration
-
additional information
additional information
-
comparison of values for various peptide substrates and enzyme sources
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
69.47
L-Arg-2-naphthylamide
-
metal-substituted enzyme form Co(II)-Ap-B, at pH 7.4 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0125
arphamemine B
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
0.024
Leucine hydroxamate
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
0.00054
leucinthiol
-
at 37°C in Bicine buffer complemented with 0.2 M NaCl
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.1
12.5
9.9
0.1
-
metal-substituted enzyme form Cu(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
12.5
-
recombinant Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
9.9
-
metal-substituted enzyme form Co(II)-Ap-B, using L-Arg-2-naphthylamide as a substrate, at pH 7.4 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme expression from embryo to adult rat, neuronal cell, developmental distribution, overview
additional information
-
cortex and anterior brain, striatum and middle brain, posterior brain
-
-
-
highest enzyme activity, mainly expressed in late spermatids during maturation
additional information
developmental expression and activity pattern of Ap-B, in-situ hydridization, overview
additional information
-
wide tissue distribution, expression level is tissue- and cell-type-dependent
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of germinal cells, proacrosmic granule of round spermatids
-
-
the enzyme is secreted, in PC-12 cells the active enzyme is associated to the external surface of the plassma mamabrane
-
-
present in secretory vesicles that contain cathepsin L with the neuropeptides enkephalin and neuropeptide Y
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AMPB_RAT
650
0
72620
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72000
74000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, citric acid-phosphate buffer or Tris-HCl buffer, 30 days, increase of activity
-
4°C, pH 6.0, 3.5% (NH4)2SO4, aggregation of monomers to polymer during storage, decomposition to monomer by substrate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose 4B column chromatography and Q-Sepharose column chromatography
-
glutathione-Sepharose 4B column chromatography and Sephadex G-150 gel filtration
-
Ni-NTA column chromatography and DEAE Trisacryl Plus M column chromatography
-
Toyopearl DEAE-650 column chromatography, Mono Q column chromatography, and DEAE-650 column chromatography
-
using a glutathione-Sepharose 4B column, cleaving of the fusion-enzyme by thrombin, using a benzamidine-Sepharose and a Q-Sepharose column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
testis enzyme, DNA and amino acid sequence determination and analysis, genetic organization and structure, overview, expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harbeson, S.L.; Rich, D.H.
Inhibition of arginine aminopeptidase by bestatin and arphamenine analogues. Evidence for a new mode of binding to aminopeptidases
Biochemistry
27
7301-7310
1988
Rattus norvegicus
Ocain, T.D.; Rich, D.H.
L-Lysinethiol: a subnanomolar inhibitor of aminopeptidase B
Biochem. Biophys. Res. Commun.
145
1038-1042
1987
Rattus norvegicus
Matsuzawa, T.; Hatsugai, M.
Effect of age on the activity of rat testicular arginine-aminopeptidase
Experientia
39
388-389
1983
Rattus norvegicus
Soederling, E.; Mkinen, K.K.
Modification of the Cl- -activated arginine aminopeptidases from rat liver and human erythrocytes: a comparative study
Arch. Biochem. Biophys.
220
11-21
1983
Homo sapiens, Rattus norvegicus
Soederling, E.
Substrate specificities of Cl- -activated arginine aminopeptidases from human and rat origin
Arch. Biochem. Biophys.
220
1-10
1983
Homo sapiens, Rattus norvegicus
Knuuttila, M.; Virtanen, K.; Soederling, E.; Maekinen, K.K.
A chloride-activated aminopeptidase in rat inflammatory exudate: properties and evidence of the origin of the enzyme
Biochem. Biophys. Res. Commun.
81
374-381
1978
Rattus norvegicus
Aoyagi, T.; Suda, H.; Nagai, M.; Ogawa, K.; Suzuki, J.; Takeuchi, T.; Umezawa, H.
Aminopeptidase activities on the surface of mammalian cells
Biochim. Biophys. Acta
452
131-143
1976
Canis lupus familiaris, Platyrrhini, Rattus norvegicus
Suda, H.; Aoyagi, T.; Takeuchi, T.; Umezawa, H.
Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer
Arch. Biochem. Biophys.
177
196-200
1976
Rattus norvegicus
Mkinen, P.L.; Mkinen, K.K.
Fractionation and properties of aminopeptidase B during purification and storage
Int. J. Pept. Protein Res.
4
241-255
1972
Rattus norvegicus
Maekinen, K.K.
Evidence for the aggregation of aminopeptidase B during storage and breakdown of the aggregate by substrate and serum albumin
Biochim. Biophys. Acta
271
413-418
1972
Rattus norvegicus
Maekinen, K.K.; Maekinen, P.L.
Evidence on erythrocyte aminopeptidase B
Int. J. Pept. Protein Res.
111
41-47
1971
Rattus norvegicus
-
Maekinen, P.L.; Raekallio, J.; Maekinen, K.K.
On the localization of aminopeptidase B and separation of its two molecular forms by automated recycling chromatography
Acta Chem. Scand.
24
1101-1102
1970
Rattus norvegicus
Maekinen, K.K.; Hopsu-Havu, V.K.
The active centre of aminopeptidase B. I. The effects of various chemical reagents
Enzymologia
32
333-346
1967
Rattus norvegicus
Maekinen, K.K.; Hopsu-Havu, V.K.
The active centre of aminopeptidase B. II. Kinetic studies
Enzymologia
32
347-363
1967
Rattus norvegicus
Hopsu, V.K.; Maekinen, K.K.; Glenner, G.G.
Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: aminopeptidase B
Arch. Biochem. Biophys.
114
557-566
1966
Rattus norvegicus
Hopsu-Havu, V.K.; Maekinen, K.K.
A simplified method for purification of rat liver aminopeptidase B
Arch. Biochem. Biophys.
118
257-258
1967
Rattus norvegicus
-
Hopsu, V.K.; Maekinen, K.K.; Glenner, G.G.
Characterization of aminopeptidase B: substrate specificity and affector studies
Arch. Biochem. Biophys.
114
567-575
1966
Rattus norvegicus
McDonald, J.K.; Barrett, A.J.
Soluble arginyl aminopeptidase
Mammalian Proteases, Academic Press
2
48-55
1986
Homo sapiens, Rattus norvegicus, Sus scrofa
-
Cadel, S.; Pierotti, A.R.; Foulon, T.; Creminon, C.; Barre, N.; Segretain, D.; Cohen, P.
Aminopeptidase B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules
Mol. Cell. Endocrinol.
110
149-160
1995
Rattus norvegicus
Cadel, S.; Foulon, T.; Viron, A.; Balogh, A.; Midol-Monnet, S.; Noel, N.; Cohen, P.
Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase
Proc. Natl. Acad. Sci. USA
94
2963-2968
1997
Rattus norvegicus (O09175)
Fukasawa, K.M.; Fukasawa, K.; Kanai, M.; Fujii, S.; Harada, M.
Molecular cloning and expression of rat liver aminopeptidase B
J. Biol. Chem.
271
30731-30735
1996
Homo sapiens, Rattus norvegicus
Petrov, V.V.; Fagard, R.H.; Lijnen, P.J.
Arginine-aminopeptidase in rat cardiac fibroblastic cells participates in angiotensin peptide turnover
Cardiovasc. Res.
61
724-735
2004
Rattus norvegicus
Piesse, C.; Cadel, S.; Gouzy-Darmon, C.; Jeanny, J.C.; Carriere, V.; Goidin, D.; Jonet, L.; Gourdji, D.; Cohen, P.; Foulon, T.
Expression of aminopeptidase B in the developing and adult rat retina
Exp. Eye Res.
79
639-648
2004
Rattus norvegicus (O09175)
Foulon, T.; Cadel, S.; Piesse, C.; Cohen, P.
Aminopeptidase B
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds) Academic Press
1
328-332
2004
Homo sapiens, Mus musculus, Rattus norvegicus
-
Agirregoitia, N.; Laiz-Carrion, R.; Varona, A.; Rio, M.P.; Mancera, J.M.; Irazusta, J.
Distribution of peptidase activity in teleost and rat tissues
J. Comp. Physiol. B
175
433-444
2005
Oncorhynchus mykiss, Rattus norvegicus, Sparus aurata
Gasparello-Clemente, E.; Casis, L.; Varona, A.; Gil, J.; Irazusta, J.; Silveira, P.F.
Aminopeptidases in visceral organs during alterations in body fluid volume and osmolality
Peptides
24
1367-1372
2003
Rattus norvegicus
Cadel, S.; Piesse, C.; Gouzy-Darmon, C.; Cohen, P.; Foulon, T.
Arginyl aminopeptidase
Proteases in Biology and Disease (Hooper, N. M. ; Lendeckel, U. ) Springer
2
113-126
2004
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
Fukasawa, K.M.; Hirose, J.; Hata, T.; Ono, Y.
Aspartic acid 405 contributes to the substrate specificity of aminopeptidase B
Biochemistry
45
11425-11431
2006
Rattus norvegicus
Hirose, J.; Ohsaki, T.; Nishimoto, N.; Matuoka, S.; Hiromoto, T.; Yoshida, T.; Minoura, T.; Iwamoto, H.; Fukasawa, K.M.
Characterization of the metal-binding site in aminopeptidase B
Biol. Pharm. Bull.
29
2378-2382
2006
Rattus norvegicus
Pham, V.L.; Cadel, M.S.; Gouzy-Darmon, C.; Hanquez, C.; Beinfeld, M.C.; Nicolas, P.; Etchebest, C.; Foulon, T.
Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling
BMC Biochem.
8
21
2007
Rattus norvegicus
Hwang, S.R.; ONeill, A.; Bark, S.; Foulon, T.; Hook, V.
Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin- and NPY-containing chromaffin granules
J. Neurochem.
100
1340-1350
2007
Rattus norvegicus, Bos taurus (A2T1U6), Bos taurus
Banegas, I.; Prieto, I.; Vives, F.; Alba, F.; de Gasparo, M.; Segarra, A.B.; Hermoso, F.; Duran, R.; Ramirez, M.
Brain aminopeptidases and hypertension
J. Renin Angiotensin Aldosterone Syst.
7
129-134
2006
Rattus norvegicus
Hui, M.; Hui, K.S.
A novel aminopeptidase with highest preference for lysine
Neurochem. Res.
31
95-102
2006
Rattus norvegicus
Hwang, S.R.; Hook, V.
Zinc regulation of aminopeptidase B involved in neuropeptide production
FEBS Lett.
582
2527-2531
2008
Rattus norvegicus
Cadel, S.; Darmon, C.; Pernier, J.; Herve, G.; Foulon, T.
The M1 family of vertebrate aminopeptidases: Role of evolutionarily conserved tyrosines in the enzymatic mechanism of aminopeptidase B
Biochimie
109
67-77
2015
Rattus norvegicus
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