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Information on EC 3.4.11.2 - membrane alanyl aminopeptidase
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3.4.11.2 membrane alanyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.2
- bestatin
-
dipeptidyl
- border
-
endopeptidase
-
brush
- angiotensin
-
carboxypeptidase
- enkephalin
- amastatin
- midguts
- sucrase
- thuringiensis
-
opioids
-
neuropeptides
- enterocytes
- maltase
-
n-acetyl-beta-d-glucosaminidase
-
gamma-glutamyl
-
nephrotoxicity
- jejunum
-
angiotensin-converting
- metallopeptidases
-
brush-border
- enkephalinase
- phosphoramidon
- captopril
-
leukotriene
- gamma-glutamyltransferase
- microvillar
- thiorphan
-
cheese
-
antinociceptive
-
ectoenzyme
- l-leucine
- sucrase-isomaltase
- leu-enkephalin
- sexta
-
dipeptidylpeptidase
- p-nitroanilide
-
3.4.24.11
-
leucyl
-
manduca
- arylamidase
- helveticus
- lta4
- coronaviruses
- dppiv
-
insulin-regulated
- disaccharidase
- oxytocinase
- medicine
- nutrition
- drug development
- analysis
- pharmacology
- diagnostics
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Synonyms
aminopeptidase n, aminopeptidase m, alanine aminopeptidase, apn/cd13, gp150, aminopeptidase-n, gp 130, alanyl aminopeptidase, aminopeptidase n/cd13, apn-1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
AlaAP
alanine aminopeptidase
alanine-specific aminopeptidase
-
-
-
-
alanyl aminopeptidase
Alpha-aminoacylpeptide hydrolase
-
-
-
-
amino-oligopeptidase
-
-
-
-
aminopeptidase M
aminopeptidase M II
-
-
-
-
aminopeptidase N
aminopeptidase, microsomal
-
-
-
-
AP-N
Ape
APN
APN1
APN2
basic aminopeptidase
beta-alanyl aminopeptidase
CD13
CryIA(C) receptor
-
-
-
-
EC 3.4.1. 2
-
-
formerly
-
EC 3.4.1.2
GP 130
-
-
-
-
GP150
L-alanine aminopeptidase
-
-
-
-
Leukemia antigen CD13
-
-
-
-
Lys-AP
-
-
-
-
Lysyl aminopeptidase
-
-
-
-
mAAP
Membrane glycoprotein H11
-
-
-
-
Membrane protein p161
-
-
-
-
Microsomal aminopeptidase
Myeloid plasma membrane glycoprotein CD13
-
-
-
-
particle-bound aminopeptidase
PepN
peptidase N
additional information
alanine aminopeptidase
-
-
-
-
alanyl aminopeptidase
-
-
-
-
aminopeptidase M
-
-
-
-
aminopeptidase N
-
-
-
-
aminopeptidase N
the enzyme has unusual specificity, cleaving adjacent to the large, nonpolar amino acids Phe and Tyr but also cleaving next to the polar residues Lys and Arg
aminopeptidase N
-
-
652749, 653002, 663607, 663608, 663873, 664281, 664466, 664501, 664688, 665112, 665146, 665231, 665240, 665244, 665708, 665710, 665832, 665955, 665958, 666148, 666532, 666997, 666998, 695577, 695995, 696753, 697036, 697250, 697299, 697302, 697386, 697396, 697439, 697497, 698298, 698381, 699938, 700617, 701038, 707702, 707799, 707956, 707961, 707970
aminopeptidase N
-
the enzyme is named aminopeptidase N because of its preference for neutral amino acids
aminopeptidase N
-
-
aminopeptidase N
-
-
APN
-
-
APN
-
-
APN1
-
-
-
-
APN2
-
-
-
-
CD13
-
-
-
-
CD13
-
-
652749, 663607, 663842, 663873, 664281, 664466, 664501, 664688, 665146, 665231, 665240, 665244, 665708, 665710, 665832, 665955, 665958, 666148, 666240, 666532, 666997, 666998, 695995, 696753, 697036, 697386, 697396, 697439, 697497, 698298, 698381, 699938, 700617, 701354, 707702, 707799, 707961, 707970
CD13
-
-
GP150
-
-
-
-
Microsomal aminopeptidase
-
-
-
-
particle-bound aminopeptidase
-
-
-
-
additional information
-
the enzyme probably belongs to the M1 family of peptidases
additional information
-
the enzyme belongs to the M1 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
-
-
-
-
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
residues E298 and Y381 located near the zinc ion, are involved in peptide cleavage. Residue M260 functions as a cushion to accept substrates with different N-terminal resiude sizes
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9054-63-1
-
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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
3-OH-L-Pro-2-NaI-7-amido-4-carbamoylmethylcoumarin + H2O
3-OH-L-Pro + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
4-Br-L-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
4-Br-L-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
4-Cl-L-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
4-Cl-L-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
4-hydroxy-2-nonenal-[Cys-Gly] conjugate + H2O
4-hydroxy-2-nonenal-[L-Cys] conjugate + glycine
-
-
-
-
?
6-O-Bzl-L-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
6-O-Bzl-L-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
7-N-(beta-alanyl)amino-1,2,4-trimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2,4-trimethyl-3H-phenoxazin-3-one + beta-alanine
7-N-(beta-alanyl)amino-1,2-dimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2-dimethyl-3H-phenoxazin-3-one + beta-alanine
7-N-(beta-alanyl)amino-1-pentylphenoxazin-3-one + H2O
alanine + 7-amino-1-pentylphenoxazin-3-one
-
chromogenic substrate
-
-
-
Ala-Phe-Tyr-Glu + H2O
Ala + Phe + Tyr + Glu
-
sequential release of N-terminal amino acids
-
-
?
aminoacyl-4-methylcoumarin 7-amide + H2O
amino acid + 7-amino-4-methylcoumarin
-
Ala-, Met-, Tyr-, Leu-, Phe-, Arg-, Lys-, Gly-, Lys-Ala-, Arg-Arg- derivatives, not: Pro-, Pyr-, Gly-Pro-derivatives
-
?
Arg-beta-naphthylamide + H2O
Arg + beta-naphthylamine
-
16.9% activity compared to Ala-beta-naphthylamide
-
-
?
beta-alanyl-7-amino-1-pentyl-3H-phenoxazin-3-one + H2O
7-amino-1-pentyl-3H-phenoxazin-3-one + beta-alanine
Boc-L-Lys-4-nitroanilide + H2O
Boc-L-Lys + 4-nitroaniline
-
21% of the activity with L-Lys-4-nitroanilide
-
-
?
Gly-7-amido-4-carbamoylmethylcoumarin + H2O
Gly + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + Gly
-
assay at pH 8.0, 37°C
-
-
?
L-2-amino-3-(2-benzothiazolyl)butyric acid-7-amido-4-carbamoylmethylcoumarin + H2O
L-2-amino-3-(2-benzothiazolyl)butyric acid + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-2-NaI-7-amido-4-carbamoylmethylcoumarin + H2O
L-2-NaI + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Abu(Bth)-7-amido-4-carbamoylmethylcoumarin + H2O
L-Abu(Bth) + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-carbamoylmethylcoumarin + H2O
L-Ala + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Ala-D-iso-Gln-meso-DAP(omegaNH2)-D-Ala-D-Ala + H2O
L-Ala + D-iso-Gln-meso-DAP(omegaNH2)-D-Ala-D-Ala
-
-
product identification and stereochemic determination
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Ala-L-Ala-L-Phe
-
assay at pH 8.0, 37°C
-
-
?
L-allyl-Gly-7-amido-4-carbamoylmethylcoumarin + H2O
L-allyl-Gly + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Arg(NO2)-7-amido-4-carbamoylmethylcoumarin + H2O
L-Arg(NO2) + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
L-Arg + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Asp(Bzl)-7-amido-4-carbamoylmethylcoumarin + H2O
L-Asp(Bzl) + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
14% of the activity with L-Ala-4-nitroanilide
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Asp
-
assay at pH 8.0, 37°C
-
-
?
L-Cha-7-amido-4-carbamoylmethylcoumarin + H2O
L-Cha + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Gln-7-amido-4-carbamoylmethylcoumarin + H2O
L-Gln + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gln
-
assay at pH 8.0, 37°C
-
-
?
L-Glu(Bzl)-7-amido-4-carbamoylmethylcoumarin + H2O
L-Glu(Bzl) + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Glu-4-nitroanilide + H2O
L-Glu + 4-nitroaniline
-
12% of the activity with L-Ala-4-nitroanilide
-
-
?
L-hArg-7-amido-4-carbamoylmethylcoumarin + H2O
L-hArg + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hCha-7-amido-4-carbamoylmethylcoumarin + H2O
L-hCha + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hLeu-7-amido-4-carbamoylmethylcoumarin + H2O
L-hLeu + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hPhe-7-amido-4-carbamoylmethylcoumarin + H2O
L-hPhe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hSer(Bzl)-7-amido-4-carbamoylmethylcoumarin + H2O
L-hSer(Bzl) + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hSer-7-amido-4-carbamoylmethylcoumarin + H2O
L-hSer + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-hTyr-7-amido-4-carbamoylmethylcoumarin + H2O
L-hTyr + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Igl-7-amido-4-carbamoylmethylcoumarin + H2O
L-Igl + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-carbamoylmethylcoumarin + H2O
L-Leu + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
assay at pH 8.0, 37°C
-
-
?
L-Lys-7-amido-4-carbamoylmethylcoumarin + H2O
L-Lys + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Met-2-naphthylamide + H2O
L-Met + 2-naphthylamine
-
8.9% of the activity with L-Ala-2-naphthylamide
-
-
?
L-Met-7-amido-4-carbamoylmethylcoumarin + H2O
L-Met + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Met
-
assay at pH 8.0, 37°C
-
-
?
L-neopentyl-Gly-7-amido-4-carbamoylmethylcoumarin + H2O
L-neopentyl-Gly + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
L-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Nva-7-amido-4-carbamoylmethylcoumarin + H2O
L-Nva + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
L-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
16.1% of the activity with L-Ala-2-naphthylamide
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Pro
-
assay at pH 8.0, 37°C
-
-
?
L-propargyl-Gly-7-amido-4-carbamoylmethylcoumarin + H2O
L-propargyl-Gly + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Ser-4-nitroanilide + H2O
L-Ser + 4-nitroaniline
-
slow activity
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Thr
-
assay at pH 8.0, 37°C
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Trp
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-4-nitroanilide + H2O
L-Tyr + 4-nitroaniline
-
-
-
-
?
L-Tyr-7-amido-4-carbamoylmethylcoumarin + H2O
L-Tyr + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Tyr
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-L-Arg + H2O
L-Tyr + L-Arg
-
best substrate among dipeptides, 57.9fold as active as L-Lys-L-Lys
-
-
?
Leu-4-methylcoumarin 7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
16% activity compared to Ala-beta-naphthylamide
-
-
?
Lys-4-methylcoumarin 7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
?
Lys-beta-naphthylamide + H2O
Lys + beta-naphthylamine
-
6.7% activity compared to Ala-beta-naphthylamide
-
-
?
Met-beta-naphthylamide + H2O
Met + beta-naphthylamine
-
8.9% activity compared to Ala-beta-naphthylamide
-
-
?
Mr 160000 component
?
-
Mr 160000 component of basement membrane, aminopeptidase N plays role in melanoma invasion of basement membrane
-
-
-
Pro-beta-naphthylamide + H2O
Pro + beta-naphthylamine
-
16.1% activity compared to Ala-beta-naphthylamide
-
-
?
VVYPWTQRF + H2O
L-Val + VYPWTQRF
-
i.e. VV-H7, fragment of human hemorphin. 43% of the activity with LVVYPWTQRF
-
-
?
VYPWTQRF + H2O
L-Val + YPWTQRF
-
i.e. V-H7, fragment of human hemorphin. 46% of the activity with LVVYPWTQRF
-
-
?
7-N-(beta-alanyl)amino-1,2,4-trimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2,4-trimethyl-3H-phenoxazin-3-one + beta-alanine
-
-
-
-
?
7-N-(beta-alanyl)amino-1,2,4-trimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2,4-trimethyl-3H-phenoxazin-3-one + beta-alanine
-
-
-
-
?
7-N-(beta-alanyl)amino-1,2-dimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2-dimethyl-3H-phenoxazin-3-one + beta-alanine
-
-
-
-
?
7-N-(beta-alanyl)amino-1,2-dimethyl-3H-phenoxazin-3-one + H2O
7-N-amino-1,2-dimethyl-3H-phenoxazin-3-one + beta-alanine
-
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + beta-naphthylamine
-
100% activity, preferred substrate
-
-
?
aminoacyl peptide
?
-
-
-
-
-
aminoacyl peptide + H2O
alanyl peptides + H2O
-
release of positively charged and uncharged amino acids from N-terminus, unable to cleave peptide bond on N-terminal side of proline residue, oligopeptides hydrolyzed faster than tri- or dipeptides, highest activity with lysyl derivatives
-
?
aminoacyl peptide + H2O
alanyl peptides + H2O
-
fast hydrolysis with Ala in N-terminal position
-
?
aminoacyl peptide + H2O
alanyl peptides + H2O
-
free alpha-amino or alpha-imino group required
-
?
aminoacyl-2-naphthylamide + H2O
amino acid + 2-naphthylamine
-
preference for substrates having hydrophobic or basic amino terminal residues with no beta-branching
-
?
aminoacyl-p-nitroanilide + H2O
amino acid + nitroaniline
-
decreasing activity in the following order: Leu- , 100%, Ala- , 88%, Met- , 77%, Lys- , 36%, Arg- , 29%, Pro- , 9%
-
?
aminoacyl-p-nitroanilide + H2O
amino acid + nitroaniline
-
-
-
?
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
ir
angiotensin III + H2O
angiotensin IV + Arg
-
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Val-Tyr-Ile-His-Pro-Phe
-
ir
beta-alanyl-7-amino-1-pentyl-3H-phenoxazin-3-one + H2O
7-amino-1-pentyl-3H-phenoxazin-3-one + beta-alanine
-
i.e. 1-pentylresorufamine
the product is a very good chromophore, having a low degree of diffusion in nutrient media for growing bacterial cultures and a bright red colour
-
?
beta-alanyl-7-amino-1-pentyl-3H-phenoxazin-3-one + H2O
7-amino-1-pentyl-3H-phenoxazin-3-one + beta-alanine
-
i.e. 1-pentylresorufamine
the product is a very good chromophore, having a low degree of diffusion in nutrient media for growing bacterial cultures and a bright red colour
-
?
beta-CN f193-209 + H2O
?
bitter peptide of aged Cheddar cheese, analysis of degradation pattern by enzyme
-
-
?
beta-CN f193-209 + H2O
?
bitter peptide of aged Cheddar cheese, analysis of degradation pattern by enzyme
-
-
?
dipeptides + H2O
amino acids
-
not: D-Ala-Gly, Val-Gly, Asp-Gly, Gly-D-Ala, Pro-containing peptides
-
?
dipeptides + H2O
amino acids
-
not: D-Ala-Gly, Val-Gly, Asp-Gly, Gly-D-Ala, Pro-containing peptides
-
?
enkephalin
?
-
may be involved in enkephalin neurotransmitter inactivation
-
-
-
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
14% of the activity with L-Ala-4-nitroanilide
-
-
?
insecticidal crystal protein
?
from Bacillus thuringensis, binds to aminopeptidase N
-
-
-
insecticidal crystal protein
?
from Bacillus thuringensis, binds to aminopeptidase N
-
-
-
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
best substrate
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
-
-
-
?
L-Ala-2-naphthylamide + H2O
L-Ala + 2-naphthylamine
-
preferred substrate
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
preferred substrate
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
best substrate
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
preferred substrate
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
663574, 663607, 663842, 665112, 665231, 665244, 665708, 665710, 665958, 666997, 683303, 683811, 683894
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
best substrate
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
-
695995, 696753, 697036, 697302, 697385, 697396, 697439, 697497, 698298, 698381, 699938, 701038, 701354
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
L-alaninyl 4-methoxy-2-naphthylamide + H2O
L-alanine + 4-methoxy-2-naphthylamine
-
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
16.9% of the activity with L-Ala-2-naphthylamide
-
-
?
L-Arg-2-naphthylamide + H2O
L-Arg + 2-naphthylamine
-
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
40% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
40% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
16.0% of the activity with L-Ala-2-naphthylamide
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
27% of the activity with L-Ala-4-nitroanilide
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
9.5% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
9.5% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-L-Arg + H2O
L-Leu + L-Arg
-
50fold as active as L-Lys-L-Lys
-
-
?
L-Leu-L-Met + H2O
L-Leu + L-Met
-
49.4fold as active as L-Lys-L-Lys
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
6.7% of the activity with L-Ala-2-naphthylamide
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
3% of the activity with L-Ala-4-nitroanilide
-
-
?
L-Lys-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin + H2O
?
-
i.e.B-9958
-
-
?
L-Lys-L-Lys-[Hyp3, CpG5, D-Tic7, CpG8]des-Arg9-bradykinin + H2O
?
-
i.e.B-9958
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
hydrolytic activity on 4-nitroanilides in decreasing order: L-Ala, L-Lys, L-Leu, L-Met, L-Gly
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
24% of the activity with L-Ala-4-nitroanilide
-
-
?
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
5.7% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-2-naphthylamide + H2O
L-Phe + 2-naphthylamine
-
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
slow activity
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
6.8% of the activity with L-Lys-4-nitroanilide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
-
-
-
?
Ser-beta-naphthylamide + H2O
Ser + beta-naphthylamine
-
1.4% activity compared to Ala-beta-naphthylamide
-
-
?
tuftsin + H2O
?
-
the first peptidic bond of this tuftsin is hydrolyzed by CD13, generating an antagonist that competes for receptor binding and thus regulating tuftsin functions
-
-
?
additional information
?
-
-
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
-
substrate specificity, overview, no activity with L-Gly-4-nitroanilide and L-Pro-4-nitroanilide, the enzyme binds to Cry1Ac toxin of Bacillus thuringiensis, not with Cry1Aa or Cey1Ab toxins, the interaction is inhibited by GalNAc
-
-
-
additional information
?
-
-
the enzyme binds the Bacillus thuringiensis Cry1Aa toxin acting as a receptor, binding site structure and localization on the enzyme determined by immunohistochemistry, overview
-
-
-
additional information
?
-
-
the enzyme prefers substrates with N-terminal nonpolar amino acids, isoyzme APN1 binds the Cry1Ac toxin from Bacillus thuringiensis via an N-acetylglucosamine moiety
-
-
-
additional information
?
-
-
L-Ser-2-naphthylamide is a poor substrate, L-Glu-2-naphthylamide is no substrate
-
-
-
additional information
?
-
-
the enzyme hydrolyzes several peptides with N-terminal L-amino acids, but not with N-terminal D-amino acids, no activity with L-Asp-L-Asp
-
-
-
additional information
?
-
-
the enzyme prefers substrates with N-terminal L-Ala residues
-
-
-
additional information
?
-
-
the enzyme plays a role in behaviour and nervous system excitability
-
-
-
additional information
?
-
-
isozyme APN1 shows preference for leucine amides, but also hydrolyzes Ile, Trp, Phe, Val, and His amides, no activity with Ser, Pro, Ala, Gly, and ARg derivatives
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
no activity with L-Val-4-nitroanilide, L-Met-4-nitroanilide, and L-Pro-4-nitroanilide
-
-
-
additional information
?
-
-
the virus receptor APN is not involved in antibody-dependent enhancement of feline infectious peritonitis virus infection
-
-
-
additional information
?
-
-
the enzyme is involved in embryonic angiogenesis and development promoting vascular growth and endothelial cell proliferation
-
-
-
additional information
?
-
Q95UF9
the aminopeptidase N3 is a putative receptor for Bacillus thuringiensis insecticidal Cry1Ac toxin
-
-
-
additional information
?
-
-
the isozymes have different roles in digestion
-
-
-
additional information
?
-
-
enzyme plays a critical role in angiogenesis
-
?
additional information
?
-
APN/CD13 plays multiple roles in morphogenesis during angiogenesis in vascular endothelium, enzyme inhibition by RNAi results in inhibition of capillary tube formation of umbilical vein endothelil cells
-
-
-
additional information
?
-
-
functional co-localization of monocytic enzyme with the Fc gamma receptors CD32 and CD64 as part of a multimeric receptor complex, overview
-
-
-
additional information
?
-
-
mechanism of APN signaling, enzyme inhibition has anti-proliferative effect and causes strong immunosuppression both in vitro and in vivo including growth arrest, induction of immunosuppressive cytokines, e.g. TGF-beta1, reduced expression of inflammatory or T-cell stimulating cytokines, e.g. interleukin-2 and interleukin-12, and mosulation of T-cell signalling pathways, overview, catalytic mechanism, ligand binding structure, active site structure, dynamic opening and closing
-
-
-
additional information
?
-
-
the ectoenzyme acts as a receptor for human coronavirus 229E, in vivo infection of primary embryonic cells and bone marrow dendritic cells
-
-
-
additional information
?
-
-
the enzyme acts as a cellsuface receptor for cells leading to rapid FcgammaRI-mediated phagocytosis of the cells, functionally interacts and partially co-localizes with FcgammaRs in monocytes, cross-linking of cells via the cytoplasmic portion of the enzyme triggers intracellular signalling, overview
-
-
-
additional information
?
-
-
the enzyme acts as receptor for the human coronavirus 229E
-
-
-
additional information
?
-
-
the enzyme can associate with tumor-associated antigen L6, TAL6, and enhance the motility of human lung cancer cells and their adhesion to extracellular matrix, overview
-
-
-
additional information
?
-
-
the enzyme expression is regulated on gingival fibroblasts in response to T-cell-derived cytokines, e.g. interleukin-4 and interleukin-13, overview
-
-
-
additional information
?
-
-
the enzyme in granulocytes may cooperate with neprilysin, the enzyme is involved in the metabolism of certain vasoactive peptides in vascular cells in the brain, the enzyme mediates human cytomegalovirus infection, the enzym regulates the cycle-dependent bioavailability of interleukin-8 in the endometrium, the enzyme's activity is regulated by estrogen
-
-
-
additional information
?
-
-
the enzyme is involved in angiogenesis and cell proliferation
-
-
-
additional information
?
-
-
the enzyme is involved in hydrolysis of neutral or basic amino acids from the N-terminus of bioactive peptides, or of amide or arylamide derivatives of amino acids, the enzyme promotes malignant angiogenesis/tumorigenesis, cell proliferation and tumor cell growth, and is involved in several diseases, e.g. inflammatory, overview, detailed catalytic machanism
-
-
-
additional information
?
-
-
the enzyme is involved in infection of cells with human cytomegalovirus and in pathogenesis, enzyme inhibition reduces the infection rate, infection induces the production of anti-CD13 antibodies, overview
-
-
-
additional information
?
-
-
the enzyme is involved in postsecretory processing of neuropeptides and peptide hormones
-
-
-
additional information
?
-
-
the enzyme is involved in signal transduction and monocytic cell adhesion mediating the binding to IgG-receptor FcgammaRs, the enzyme expression is down-regulated during homotypic aggregation, while the enzyme induced the homoypic aggregation, overview
-
-
-
additional information
?
-
-
the enzyme might contribute to extracellular matrix degradation, the enzyme shows increased surface expression in cases of malignant transformation, inflamation, or T-cell activation
-
-
-
additional information
?
-
-
the enzyme negatively regulates tumor necrosis factor-alpha-induced apoptosis in human neutrophils via inhibition of TNF receptor I shedding, mechanism, overview
-
-
-
additional information
?
-
-
the enzyme plays a role in the modulation of kinins, neuropeptides, and chemotactic mediators as well as in adhesion and cell-cell interactions, it participates in antigen processing and presentation, trimming of peptides protrusing out of MHC class II molecules, and acts in inflammatory processes, interleukin-10 and TGF-beta are involved in enzyme upregulation in monocytes and U-937 cells, overview
-
-
-
additional information
?
-
-
the enzyme plays an important role in tumor cell invasion, the enzyme regulation involves the basic fibroblast growth factor
-
-
-
additional information
?
-
-
the enzyme serves as receptor for coronaviruses, modulates bioactive peptide responses, e.g. vasopressin release, and influences immune functions and major biological processess, such as cell proliferation, secretion, invasion, and angiogenesis, overview, enzyme inhibition affects these processes, overview
-
-
-
additional information
?
-
-
the inhibition of APN results in decreased growth of cultured keratinocytes
-
-
-
additional information
?
-
-
the membrane enzyme is involved in keratinocyte growth and differentiation, inhibition of the enzyme contributes to inhibition of DNA synthesis in proliferating cells
-
-
-
additional information
?
-
-
enzyme inhibition causes strong immunosuppression both in vitro and in vivo
-
-
-
additional information
?
-
-
substrate specificity, overview, chain length influencs the activity rate, dipeptides are readily hydrolyzed, the enzyme prefers substrates with N-terminal L-Ala residues, the specificity for N-terminal residues is descending order is Ala, Phe, Tyr, Leu, Arg, Thr, Trp, Lys, Ser, Asp, His, Val. Pro- and alpha- or gamma-Glu-derivatives are slowly hydrolyzed, when a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
-
-
-
additional information
?
-
-
the enzyme prefers neutral N-terminal amino acid substrates
-
-
-
additional information
?
-
-
role for CD13 in plasma membrane organization. Peptidase activity of CD13 is required for this regulatory activity
-
-
-
additional information
?
-
-
where initial removal of the NH2-terminal dipeptide from CXCL11 by CD26 allows for further truncation by CD13
-
-
-
additional information
?
-
-
aminopeptidase N removes N-terminal amino acids from unsubstituted oligopeptides, amide or arylamide, with the exception of peptides with Pro in the penultimate position, the order of favored substrates is Ala>Phe>Tyr>Leu>Arg>Thr>Trp>Lys> Ser>Asp>His>Val
-
-
-
additional information
?
-
-
CD13 degrades the chemokine CXCL11, downregulates CXCR4 and modulates stromal cell-derived factor-1 (also known as CXCL12)-induced migration
-
-
-
additional information
?
-
-
CD13 hydrolyzes synthetic oligopeptides corresponding to the N terminus of interleukin-1a, interleukin-1b and interleukin-2, although natural interleukin-2 and G-CSF are resistant to hydrolysis
-
-
-
additional information
?
-
-
CD13 is a receptor for human coronavirus 229E and human cytomegalovirus
-
-
-
additional information
?
-
-
in vitro, CD13 participates in the metabolism of glutathione, somatostatin, thymopentin, neurokinin A, splenopentin, nociceptin (orphanin) FQ, and peptides derived from the thrombin receptor
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues
-
-
-
additional information
?
-
-
the enzyme acts as major receptor for the CryIAc toxin of Bacillus thuringiensis
-
-
-
additional information
?
-
-
Cry1AC toxin induces APN shedding from midgut epithelial cells into the luminal fluid, and depletion of the membrane-anchored enzyme on the midgut epithelial cells
-
-
-
additional information
?
-
-
the enzyme binds the Cry1Ac toxin from Bacillus thuringiensis
-
-
-
additional information
?
-
-
substrate specificity, the enzyme prefers substrates with Ala or Met residues at the N-terminus, overview
-
-
-
additional information
?
-
-
insulin affects the lysosomal enzyme activity in kidney and liver, overview
-
-
-
additional information
?
-
-
the enzyme is involved in infection of cells with murine cytomegalovirus and in pathogenesis, enzyme inhibition reduces the infection rate, infection induces the production of anti-CD13 antibodies, overview
-
-
-
additional information
?
-
-
no activity with 4-nitroanilides of Pro, Ile, Val, and Phe
-
-
-
additional information
?
-
-
substrate specificity, overview, chain length influencs the activity rate, dipeptides are readily hydrolyzed, the enzyme prefers substrates with N-terminal L-Ala residues, the specificity for N-terminal residues is descending order is Ala, Phe, Tyr, Leu, Arg, Thr, Trp, Lys, Ser, Asp, His, Val. Pro- and alpha- or gamma-Glu-derivatives are slowly hydrolyzed, when a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Ala, Arg, Lys or Leu residues
-
-
-
additional information
?
-
-
synthesis and activity of chromogenic phenoxazinone substrates, phenoxazinones are the chromophores in a number of synthetic dyestuffs and natural coloured matters and the phenoxazinone chromophore has been found in a number of mould metabolites and other natural products, overview
-
-
-
additional information
?
-
-
synthesis and activity of chromogenic phenoxazinone substrates, phenoxazinones are the chromophores in a number of synthetic dyestuffs and natural coloured matters and the phenoxazinone chromophore has been found in a number of mould metabolites and other natural products, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Ala, Arg, Lys or Leu residues
-
-
-
additional information
?
-
-
the enzyme is involved in hematopoiesis and bone growth, increased enzyme expression occurs during angiogenesis associated with cancer development
-
-
-
additional information
?
-
-
substrate specificity, overview, chain length influencs the activity rate, dipeptides are readily hydrolyzed, the enzyme prefers substrates with N-terminal L-Ala residues, the specificity for N-terminal residues is descending order is Ala, Phe, Tyr, Leu, Arg, Thr, Trp, Lys, Ser, Asp, His, Val. Pro- and alpha- or gamma-Glu-derivatives are slowly hydrolyzed, when a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide
-
-
-
additional information
?
-
-
no activity with N-terminal Leu-substrates
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
broad substrate specificity, the enzyme prefers N-terminal alkaline and aliphatic amino acid substrates showing high activity with peptides possessing N-terminal Lys or Leu residues and, to a lesser extent, Ala residues
-
-
-
additional information
?
-
-
the enzyme might be involved in the turnover of intracellular peptides
-
-
-
additional information
?
-
-
no activity with L-Val-4-nitroanilide, L-Glu-4-nitroanilide, and L-Asp-4-nitroanilide, no activity with N-alpha-benzoyl-L-Arg-2-naphthylamide
-
-
-
additional information
?
-
-
no hydrolysis of Lys-Pro and Pro-Phe bond
-
-
-
additional information
?
-
-
no hydrolysis of Lys-Pro and Pro-Phe bond
-
-
-
additional information
?
-
-
the brain enzyme is involved in termination of the action of neuropeptides, especially of enkephalins and angiotensin III, the kidney enzyme contributes to the extracellular catabolism of glutathione, the intestinal enzyme acts as a receptor for the transmissible gastroenteritis virus, a coronavirus, causing fatal diarrhea in newborn pigs
-
-
-
additional information
?
-
-
the enzyme activity in muscle decreases during Jinhua ham processing, e.g. salting, with increasing levels of free amino acids which is important for the ham flavor, overview
-
-
-
additional information
?
-
-
the enzyme plays a key role in tumor cell invasion and angiogenesis, enzyme inhibition by psammaplin A suppresses the invasion and tube formation of endothelial cells stimulated by basic fibroblast growth factor, and proliferation of cancer and endothelial cells, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, chain length influencs the activity rate, dipeptides are readily hydrolyzed, the enzyme prefers substrates with N-terminal L-Ala residues, the specificity for N-terminal residues is descending order is Ala, Phe, Tyr, Leu, Arg, Thr, Trp, Lys, Ser, Asp, His, Val. Pro- and alpha- or gamma-Glu-derivatives are slowly hydrolyzed, when a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. Glu350 is involved in catalysis, the enzyme in lung is identical with the p146 type II alveolar epithelial cell antigen
-
-
-
additional information
?
-
-
in combination with CD26/dipeptidyl peptidase IV, aminopeptidase N processes chemokine ligand CXCL11, but not CXCL8, to generate truncated CXCL11 forms. The truncated CXCL11 fails to induce an intracellular calcium increase but is still able to bind and desensitize CXCR3 for intact CXCL11 signaling. Truncated CXCL11 fails to attract lymphocytes, and further processing by aminopeptidase N results in significant reduction of inhibition of HMVEC migration
-
-
-
additional information
?
-
-
no substrate: YPWTQRF, i.e. fragment H7 of human hemorphin
-
-
-
additional information
?
-
-
broad substrate specificity for N-terminal amino acid residues, no activity with Asp-2-naphthylamide, the enzyme prefers tri- and tetrapeptides to di- and pentapeptides
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
angiotensin III + H2O
angiotensin IV + Arg
-
the enzyme is involved in regulation of blood pressure in the renin-angiotensin system in the brain causing hypertension, the enzyme is involved in metabolism of angiotensin II and angiotensin III in the brain, overview
-
-
ir
Mr 160000 component
?
-
Mr 160000 component of basement membrane, aminopeptidase N plays role in melanoma invasion of basement membrane
-
-
-
aminoacyl peptide
?
-
-
-
-
-
enkephalin
?
-
may be involved in enkephalin neurotransmitter inactivation
-
-
-
insecticidal crystal protein
?
P91885
from Bacillus thuringensis, binds to aminopeptidase N
-
-
-
insecticidal crystal protein
?
P91887
from Bacillus thuringensis, binds to aminopeptidase N
-
-
-
additional information
?
-
-
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
C5H690
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
C5H690
APN is a specific binding protein, and a putative midgut receptor, for Bacillus thuringiensis Cry11Ba toxin
-
-
-
additional information
?
-
-
the enzyme plays a role in behaviour and nervous system excitability
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the virus receptor APN is not involved in antibody-dependent enhancement of feline infectious peritonitis virus infection
-
-
-
additional information
?
-
-
the enzyme is involved in embryonic angiogenesis and development promoting vascular growth and endothelial cell proliferation
-
-
-
additional information
?
-
Q95UF9
the aminopeptidase N3 is a putative receptor for Bacillus thuringiensis insecticidal Cry1Ac toxin
-
-
-
additional information
?
-
-
the isozymes have different roles in digestion
-
-
-
additional information
?
-
-
enzyme plays a critical role in angiogenesis
-
?
additional information
?
-
P15144
APN/CD13 plays multiple roles in morphogenesis during angiogenesis in vascular endothelium, enzyme inhibition by RNAi results in inhibition of capillary tube formation of umbilical vein endothelil cells
-
-
-
additional information
?
-
-
functional co-localization of monocytic enzyme with the Fc gamma receptors CD32 and CD64 as part of a multimeric receptor complex, overview
-
-
-
additional information
?
-
-
mechanism of APN signaling, enzyme inhibition has anti-proliferative effect and causes strong immunosuppression both in vitro and in vivo including growth arrest, induction of immunosuppressive cytokines, e.g. TGF-beta1, reduced expression of inflammatory or T-cell stimulating cytokines, e.g. interleukin-2 and interleukin-12, and mosulation of T-cell signalling pathways, overview, catalytic mechanism, ligand binding structure, active site structure, dynamic opening and closing
-
-
-
additional information
?
-
-
the ectoenzyme acts as a receptor for human coronavirus 229E, in vivo infection of primary embryonic cells and bone marrow dendritic cells
-
-
-
additional information
?
-
-
the enzyme acts as a cellsuface receptor for cells leading to rapid FcgammaRI-mediated phagocytosis of the cells, functionally interacts and partially co-localizes with FcgammaRs in monocytes, cross-linking of cells via the cytoplasmic portion of the enzyme triggers intracellular signalling, overview
-
-
-
additional information
?
-
-
the enzyme acts as receptor for the human coronavirus 229E
-
-
-
additional information
?
-
-
the enzyme can associate with tumor-associated antigen L6, TAL6, and enhance the motility of human lung cancer cells and their adhesion to extracellular matrix, overview
-
-
-
additional information
?
-
-
the enzyme expression is regulated on gingival fibroblasts in response to T-cell-derived cytokines, e.g. interleukin-4 and interleukin-13, overview
-
-
-
additional information
?
-
-
the enzyme in granulocytes may cooperate with neprilysin, the enzyme is involved in the metabolism of certain vasoactive peptides in vascular cells in the brain, the enzyme mediates human cytomegalovirus infection, the enzym regulates the cycle-dependent bioavailability of interleukin-8 in the endometrium, the enzyme's activity is regulated by estrogen
-
-
-
additional information
?
-
-
the enzyme is involved in angiogenesis and cell proliferation
-
-
-
additional information
?
-
-
the enzyme is involved in hydrolysis of neutral or basic amino acids from the N-terminus of bioactive peptides, or of amide or arylamide derivatives of amino acids, the enzyme promotes malignant angiogenesis/tumorigenesis, cell proliferation and tumor cell growth, and is involved in several diseases, e.g. inflammatory, overview, detailed catalytic machanism
-
-
-
additional information
?
-
-
the enzyme is involved in infection of cells with human cytomegalovirus and in pathogenesis, enzyme inhibition reduces the infection rate, infection induces the production of anti-CD13 antibodies, overview
-
-
-
additional information
?
-
-
the enzyme is involved in postsecretory processing of neuropeptides and peptide hormones
-
-
-
additional information
?
-
-
the enzyme is involved in signal transduction and monocytic cell adhesion mediating the binding to IgG-receptor FcgammaRs, the enzyme expression is down-regulated during homotypic aggregation, while the enzyme induced the homoypic aggregation, overview
-
-
-
additional information
?
-
-
the enzyme might contribute to extracellular matrix degradation, the enzyme shows increased surface expression in cases of malignant transformation, inflamation, or T-cell activation
-
-
-
additional information
?
-
-
the enzyme negatively regulates tumor necrosis factor-alpha-induced apoptosis in human neutrophils via inhibition of TNF receptor I shedding, mechanism, overview
-
-
-
additional information
?
-
-
the enzyme plays a role in the modulation of kinins, neuropeptides, and chemotactic mediators as well as in adhesion and cell-cell interactions, it participates in antigen processing and presentation, trimming of peptides protrusing out of MHC class II molecules, and acts in inflammatory processes, interleukin-10 and TGF-beta are involved in enzyme upregulation in monocytes and U-937 cells, overview
-
-
-
additional information
?
-
-
the enzyme plays an important role in tumor cell invasion, the enzyme regulation involves the basic fibroblast growth factor
-
-
-
additional information
?
-
-
the enzyme serves as receptor for coronaviruses, modulates bioactive peptide responses, e.g. vasopressin release, and influences immune functions and major biological processess, such as cell proliferation, secretion, invasion, and angiogenesis, overview, enzyme inhibition affects these processes, overview
-
-
-
additional information
?
-
-
the inhibition of APN results in decreased growth of cultured keratinocytes
-
-
-
additional information
?
-
-
the membrane enzyme is involved in keratinocyte growth and differentiation, inhibition of the enzyme contributes to inhibition of DNA synthesis in proliferating cells
-
-
-
additional information
?
-
-
role for CD13 in plasma membrane organization. Peptidase activity of CD13 is required for this regulatory activity
-
-
-
additional information
?
-
-
where initial removal of the NH2-terminal dipeptide from CXCL11 by CD26 allows for further truncation by CD13
-
-
-
additional information
?
-
-
aminopeptidase N removes N-terminal amino acids from unsubstituted oligopeptides, amide or arylamide, with the exception of peptides with Pro in the penultimate position, the order of favored substrates is Ala>Phe>Tyr>Leu>Arg>Thr>Trp>Lys> Ser>Asp>His>Val
-
-
-
additional information
?
-
-
CD13 degrades the chemokine CXCL11, downregulates CXCR4 and modulates stromal cell-derived factor-1 (also known as CXCL12)-induced migration
-
-
-
additional information
?
-
-
CD13 hydrolyzes synthetic oligopeptides corresponding to the N terminus of interleukin-1a, interleukin-1b and interleukin-2, although natural interleukin-2 and G-CSF are resistant to hydrolysis
-
-
-
additional information
?
-
-
CD13 is a receptor for human coronavirus 229E and human cytomegalovirus
-
-
-
additional information
?
-
-
in vitro, CD13 participates in the metabolism of glutathione, somatostatin, thymopentin, neurokinin A, splenopentin, nociceptin (orphanin) FQ, and peptides derived from the thrombin receptor
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme acts as major receptor for the CryIAc toxin of Bacillus thuringiensis
-
-
-
additional information
?
-
-
Cry1AC toxin induces APN shedding from midgut epithelial cells into the luminal fluid, and depletion of the membrane-anchored enzyme on the midgut epithelial cells
-
-
-
additional information
?
-
-
insulin affects the lysosomal enzyme activity in kidney and liver, overview
-
-
-
additional information
?
-
-
the enzyme is involved in infection of cells with murine cytomegalovirus and in pathogenesis, enzyme inhibition reduces the infection rate, infection induces the production of anti-CD13 antibodies, overview
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the transport and degradation of extracellular peptides, aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme is involved in hematopoiesis and bone growth, increased enzyme expression occurs during angiogenesis associated with cancer development
-
-
-
additional information
?
-
-
aminopeptidase regulation mechanisms and biological functions, overview
-
-
-
additional information
?
-
-
the enzyme might be involved in the turnover of intracellular peptides
-
-
-
additional information
?
-
-
the brain enzyme is involved in termination of the action of neuropeptides, especially of enkephalins and angiotensin III, the kidney enzyme contributes to the extracellular catabolism of glutathione, the intestinal enzyme acts as a receptor for the transmissible gastroenteritis virus, a coronavirus, causing fatal diarrhea in newborn pigs
-
-
-
additional information
?
-
-
the enzyme activity in muscle decreases during Jinhua ham processing, e.g. salting, with increasing levels of free amino acids which is important for the ham flavor, overview
-
-
-
additional information
?
-
-
the enzyme plays a key role in tumor cell invasion and angiogenesis, enzyme inhibition by psammaplin A suppresses the invasion and tube formation of endothelial cells stimulated by basic fibroblast growth factor, and proliferation of cancer and endothelial cells, overview
-
-
-
additional information
?
-
-
in combination with CD26/dipeptidyl peptidase IV, aminopeptidase N processes chemokine ligand CXCL11, but not CXCL8, to generate truncated CXCL11 forms. The truncated CXCL11 fails to induce an intracellular calcium increase but is still able to bind and desensitize CXCR3 for intact CXCL11 signaling. Truncated CXCL11 fails to attract lymphocytes, and further processing by aminopeptidase N results in significant reduction of inhibition of HMVEC migration
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
Cu2+
F9W8I6, G0UZY5
10 mM, leads to complete inhibition; 10 mM, relative activity: 12%, compared to no cation: 100%
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
F9W8I6, G0UZY5
10 mM, relative activity: 121%, compared to no cation: 100%; 10 mM, relative activity: 137%, compared to no cation: 100%
Co2+
F9W8I6, G0UZY5
10 mM, relative activity: 151%, compared to no cation: 100%; 10 mM, relative activity: 84%, compared to no cation: 100%
Fe2+
F9W8I6, G0UZY5
10 mM, relative activity: 126%, compared to no cation: 100%; 10 mM, relative activity: 139%, compared to no cation: 100%
Mg2+
F9W8I6, G0UZY5
10 mM, relative activity: 107%, compared to no cation: 100%; 10 mM, relative activity: 149%, compared to no cation: 100%
Mn2+
F9W8I6, G0UZY5
10 mM, relative activity: 140%, compared to no cation: 100%; 10 mM, relative activity: 158%, compared to no cation: 100%
Ni2+
F9W8I6, G0UZY5
10 mM, relative activity: 133%, compared to no cation: 100%; 10 mM, relative activity: 141%, compared to no cation: 100%
Zn2+
-
content: 0.72 mol/mol protein; increase of activity at concentrations below 0.1 mM
Zn2+
enzyme contains a consensus zinc-binding/gluzincin motif HEXXHX18E, residues 371-394
Zn2+
-
at concentrations between 0.1 and 0.3 mM reactivation after inhibition by 1,10-phenanthroline, inhibitory at higher concentrations
Zn2+
-
the enzyme possesses a central Zn2+ coordination site H1EXXHX18E24
Zn2+
-
zinc-metalloendopeptidase, contains the conserved zinc-binding motif HEXXH, i.e. HEALH-X18E, binds to the active site
Zn2+
-
dependent on
Zn2+
enzyme contains a consensus zinc-binding/gluzincin motif HEXXHX18E
Zn2+
-
the enzyme contains a typical zinc-binding motif HEXXH, one Zn2+ per subunit
Zn2+
F9W8I6, G0UZY5
10 mM, relative activity: 117%, compared to no cation: 100%; 10 mM, relative activity: 84%, compared to no cation: 100%
additional information
-
metallopeptidase, no or poor inhibition by Co2+ and Mg2+
additional information
metallopeptidase, no or poor inhibition by Co2+ and Mg2+
additional information
-
the enzyme is not affected by Ca2+, Zn2+, and Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-benzyl-1H-imidazol-4-yl)methyl 6-oxidanyl-6-oxidanylidene-N-[(3,4,5-trimethoxyphenyl)carbonyl]-L-norleucylalaninate
-
-
(1S)-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
-
IC50: 70 nM
(1S)-2-phenyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)ethanaminium acetate
-
IC50: 50 nM
(1S)-3-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)butan-1-aminium acetate
-
IC50: 74 nM
(2E)-N-[(2R)-2-amino-3-phenylpropyl]-3-(3,4-dihydroxyphenyl)-acrylamide hydrochloride
-
-
(2E,2'E)-N,N'-[disulfanediyldi(ethane-2,1-diyl)]bis[3-(3-bromo-4-hydroxyphenyl)-2-(hydroxyimino)propanamide]
-
PsA, isolated from a marine sponge, inhibits the enzyme non-competitively and suppresses angiogenesis in vitro, IC50 is 0.018 mM
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-bromophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-chlorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-fluorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-methoxyphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrophenyl)-1,3,4-thiadiazol-2-yl]-2-[(cinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-coumaroyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrophenyl)-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(benzoyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylacetyl)amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)-amino]-propanamide
-
-
(2R)-N-[5-(4-nitrorophenyl)-1,3,4-thiadiazol-2-yl]-2-[(phenylsulfonyl)amino]-propanamide
-
-
(2R)-N-[5-phenyl-1,3,4-thiadiazol-2-yl]-2-[(p-methoxycinnamoyl)amino]-propanamide
-
-
(2R,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
moderate APN inhibition
(2R,3S)-2-amino-3-hydroxy-N-((S)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl)-3-(4-nitrophenyl)propanamide
-
-
(2R,3S)-2-amino-3-hydroxy-N-((S)-1-hydroxy-3-phenylpropan-2-yl)-3-(4-nitrophenyl)propanamide
-
-
(2R,3S)-2-amino-3-hydroxy-N-(4-hydroxyphenethyl)-3-(4-nitrophenyl) propanamide
-
-
(2R,3S)-2-amino-N-(2-(benzo[d][1,3]dioxol-5-yl)ethyl)-3-hydroxy-3-(4-nitrophenyl)propanamide
-
-
(2S)-2-amino-3-hydroxyl-N-[(2R)-2-amino-3-phenylpropyl]propionamide hydrochloride
-
-
(2S)-2-amino-3-methyl-N-[(2R)-2-amino-3-phenylpropyl]propionamide hydrochloride
-
-
(2S)-2-amino-3-thiol-N-[(2R)-2-amino-3-phenylpropyl]propionamide hydrochloride
-
-
(2S)-2-amino-4-methylthio-N-[(2R)-2-amino-3-phenylpropyl]butyramide hydrochloride
-
-
(2S)-2-amino-N-[(3S)-1-[2-(hydroxyamino)-2-oxoethyl]-2,6-dioxopiperidin-3-yl]-3-phenylpropanamide
-
-
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl-L-prolyl-(trans-4-hydroxy-L-proline)
-
i.e. MR387A
(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl-L-prolyl-L-proline
-
i.e. MR378B
(2S,3R)-3-amino-2-hydroxy-N-1H-imidazo[4,5-c]pyridin-4-yl-4-phenylbutanamide
-
-
(2S,3R)-3-amino-N-(2,6-dihydroxypyrimidin-4-yl)-2-hydroxy-4-phenylbutanamide
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(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(2-phenylethyl)oxime hydrochloride
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(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(3-phenylpropyl)oxime hydrochloride
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(2Z)-3-amino-3,4-dihydronaphthalen-2(1H)-one O-(4-phenylbutyl)oxime hydrochloride
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(3S)-3-(D-alanylamino)-2-([[(1S)-1-aminoethyl][(3r)-tricyclo[3.3.1.13,7]dec-1-yloxy]phosphoryl]methyl)-5-methylhexanoic acid
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(3S)-N-hydroxy-2-(phenylsulfonyl)-6,10-dioxa-2-azaspiro[4.5]decane-3-carboxamide
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(3S)-N-hydroxy-2-(phenylsulfonyl)-6,11-dioxa-2-azaspiro[4.6]undecane-3-carboxamide
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(3S)-N-hydroxy-2-(phenylsulfonyl)-6,12-dioxa-2-azaspiro[4.7]dodecane-3-carboxamide