3.4.11.1: leucyl aminopeptidase
This is an abbreviated version!
For detailed information about leucyl aminopeptidase, go to the full flat file.
Word Map on EC 3.4.11.1
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3.4.11.1
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aminopeptidases
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border
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brush
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bestatin
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transpeptidase
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gamma-glutamyl
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maltase
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carboxypeptidase
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sucrase
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urinary
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pregnancy
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bile
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urine
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esterase
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mucosa
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trim
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chymotrypsin
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transaminase
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dipeptidyl
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beta-glucuronidase
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5'-nucleotidase
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exopeptidase
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brush-border
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histocompatibility
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bilirubin
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nephrotoxicity
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gamma-glutamyltransferase
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alanyl
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ankylosing
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spondylitis
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arylamidase
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jaundice
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p-nitroanilide
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canalicular
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hepatobiliary
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n-acetyl-beta-glucosaminidase
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gamma-glutamyltranspeptidase
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dipeptidase
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disaccharidase
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oxytocinase
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gamma-gtp
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cholinesterase
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3.4.11.2
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amastatin
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trehalase
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hepatica
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cellobiohydrolase
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peptidome
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fasciola
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enzymuria
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medicine
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synthesis
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pharmacology
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food industry
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drug development
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diagnostics
- 3.4.11.1
- aminopeptidases
- border
-
brush
- bestatin
- transpeptidase
-
gamma-glutamyl
- maltase
- carboxypeptidase
- sucrase
- urinary
- pregnancy
- bile
- urine
- esterase
- mucosa
-
trim
- chymotrypsin
- transaminase
-
dipeptidyl
- beta-glucuronidase
- 5'-nucleotidase
-
exopeptidase
-
brush-border
-
histocompatibility
- bilirubin
-
nephrotoxicity
- gamma-glutamyltransferase
-
alanyl
-
ankylosing
- spondylitis
- arylamidase
-
jaundice
- p-nitroanilide
-
canalicular
- hepatobiliary
- n-acetyl-beta-glucosaminidase
- gamma-glutamyltranspeptidase
- dipeptidase
- disaccharidase
- oxytocinase
- gamma-gtp
- cholinesterase
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3.4.11.2
- amastatin
- trehalase
- hepatica
- cellobiohydrolase
-
peptidome
- fasciola
-
enzymuria
- medicine
- synthesis
- pharmacology
- food industry
- drug development
- diagnostics
Reaction
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low =
Synonyms
A-LAP, acidic M17 leucine aminopeptidase, AcLAP, adipocyte-derived leucine aminopeptidase, Aminopeptidase, aminopeptidase A, Aminopeptidase A/I, aminopeptidase I, aminopeptidase II, Aminopeptidase III, aminopeptidase LAP2, aminopeptidase N, AP 28, AP 56, APDkam589, APN, b/LAP, bovine lens/leucine aminopeptidase, BSAP, cathepsin III, CsLAP1, CsLAP2, cysteinyl-glycine hydrolysing activity, cysteinylglycine-hydrolysing activity, cytosol aminopeptidase, DR57, EC 3.4.1.1, Eg-LAP, endoplasmic reticulum aminopeptidase, ER-aminopeptidase-1, ERAP, ERAP1, ERAP2, FgLAP, FrvX, FTBL protein, FTBL proteins, HSA, L-leucine aminopeptidase, la, LAP, LAP yspII, LAP-A, LAP-N, LAP1, LAP2, lap3, LapA, LAPc, LeuAP, leucinamide aminopeptidase, leucinaminopeptidase, leucine amino peptidase, leucine aminopeptidase, leucine aminopeptidase 1, leucine aminopeptidase 2, leucine aminopeptidase 3, leucine aminopeptidase A, leucine aminopeptidase LAP-N, leucine aminopeptidase N, leucine aminopeptidase,, leucine aminopeptidase-A, Leucyl aminopeptidase, leucyl aminopeptidase (animal), leucyl aminopeptidase (plant), leucyl aminopeptidase yspII, leucyl peptidase, leucylaminopeptidase, leucylpeptidase, LmLAP-A, M17 family leucyl aminopeptidase metalloprotease, M17 LAP, M17 leucine amino peptidase, M17 leucine aminopeptidase, M17 leucyl aminopeptidase, M42 aminopeptidase, major leucyl aminopeptidase, More, PA2939, PaAP, PepA, PepA peptidase A, PepB, peptidase B, peptidase II, peptidase S, pepZ, PfLAP, PH1527, PhTET2, PILS-AP, PILSAP, Placental leucine aminopeptidase, PLAP, proline aminopeptidase, Prolyl aminopeptidase, proteins, specific or class, FTBL, PtLAP, puromycin insensitive leucyl-specific aminopeptidase, puromycin-insensitive leucine specific aminopeptidase, puromycin-insensitive leucyl-specific aminopeptidase, PVX_118180, rLAP, rMHJ_0461, S-Lap1, S-Lap2, S-Lap3, S-Lap4, S-Lap5, S-Lap6, S-Lap7, S-Lap8, SmLAP1, SmLAP2, Smp_03000, Smp_083870, sperm-leucylaminopeptidase, TbLAP-A, TbLAP1, TcLAP-A, TM0042, TpLAP, XoLAP
ECTree
3.4.11.1 leucyl aminopeptidaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.11.1 - leucyl aminopeptidase
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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 II + H2O
Asp + angiotensin III
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i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
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?
Cys-Gly + H2O
Cys + Gly
the enzyme plays a role in glutathione turnover
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?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
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?
phosphatidylinositol-dependent kinase-1 + H2O
?
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i.e. PDK1, removal of 9 amino acids from the N-terminus of the kinase, which allows S6 kinase to associate with PDK1 and the enzyme upon vascular endothelial growth factor stimulation
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?
cysteinylglycine + H2O
cysteine + glycine
involved in turnover of glutathione
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?
cysteinylglycine + H2O
cysteine + glycine
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involved in the metabolism of glutathione and glutathione S-conjugates, major cysteinylglycine-hydrolysing activity
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?
additional information
?
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the enzyme has tissue-specifici physiological roles, overview, active site structure and zinc-binding, mechanism
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?
additional information
?
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enzyme activity is regulated on the transcriptional level
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?
additional information
?
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broad substrate specificity towards naturally occurring peptide hormones, while the enzyme hydrolyzes synthetic substrate in vitro with specificity for leucine, enzyme plays a role in regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney
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?
additional information
?
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A-LAP plays a key role in the MHC class I antigen-presentation pathway, the enzyme is involved in the renin-angiotensin-system, RAS, and angiotensin II metabolism, and plays a role in blood pressure decrease through inactivation of angiotensin II, overview
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?
additional information
?
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the enzyme has tissue-specifici physiological roles, e.g. trimmíng of the N-terminus of antigenic peptides for presentation or in eye cataract, overview
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?
additional information
?
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the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
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?
additional information
?
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the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
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?
additional information
?
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the enzyme is involved in processing of precursor peptides, and in destruction of antigenic peptides to limit antigen presentation to MHC class I molecules in the endoplasmic reticulum lumen, pathway overview
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?
additional information
?
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the enzyme is required for DNA synthesis and plays an important role in angiogenesis by regulating the proliferation and migration of endothelial cells, mechanism via vascular endothelial growth factor and stimulation of S6 kinase, overview
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?
additional information
?
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PILSAP is required for the development of vascular as well as hematopoietic system in embryoid bodies
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?
additional information
?
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the enzyme affects RhoA activation and that influences the proper function of endothelial cells
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?
additional information
?
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MHJ_0461 binds heparin and interacts with DNA
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?
additional information
?
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MHJ_0461 binds heparin and interacts with DNA
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?
additional information
?
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rMHJ_0461 binds plasminogen and facilitates plasmin conversion
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?
additional information
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rMHJ_0461 binds plasminogen and facilitates plasmin conversion
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?
additional information
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alterations in intensity and number of isozymes in cold-acclimated plants, bark and leaf
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?
additional information
?
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the enzyme is important in the generation and regulation of free amino acids that are used in protein anabolism and for maintaining osmotic stability within the infected erythrocyte, enzyme inhibition, e.g. by bestatin, blocks intraerythrocytic development of malaria parasites
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?
additional information
?
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the enzyme functions in the terminal stages of hemoglobin digestion
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?
additional information
?
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the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
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?
additional information
?
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the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
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?
additional information
?
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the enzyme functions in the terminal stages of hemoglobin digestion
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?
additional information
?
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the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
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?
additional information
?
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the enzyme generates and regulates the internal pool of free amino acids and therefore represents a target for antimalarial drugs
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?
additional information
?
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M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation
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?
additional information
?
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M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation
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?
additional information
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proteolysis of ACTH-(6-9)-PGP peptide in rat blood and plasma occurs mainly under the effect of enzymes whose action is similar to leucine aminopeptidase
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?
additional information
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proteolysis of ACTH-(6-9)-PGP peptide in rat blood and plasma occurs mainly under the effect of enzymes whose action is similar to leucine aminopeptidase
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?
additional information
?
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no growth on QL, FL, YL, WL, IL, VL, KL, GL, RL, and PL
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?
additional information
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the enzyme probably is involved in fertility and parasite survival
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?
additional information
?
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the enzyme has tissue-specifici physiological roles, overview
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?
additional information
?
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PepA functions as a transcriptional repressor in regulatory cascade that controls virulence gene expression in Vibrio cholerae
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?
