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Information on EC 3.4.11.22 - aminopeptidase I and Organism(s) Saccharomyces cerevisiae and UniProt Accession P14904

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.22 aminopeptidase I
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P14904 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates
Synonyms
erap1, aminopeptidase i, endoplasmic reticulum aminopeptidase 1, leucine-aminopeptidase, eraap, endoplasmic reticulum aminopeptidase, a-lap, arts-1, aminopeptidase 1, lapase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Actinase AS
-
-
-
-
alpha-Aminoacyl-peptide hydrolase
-
-
-
-
Aminooligopeptidase
-
-
-
-
Aminopeptidase
-
-
-
-
aminopeptidase 1
-
-
aminopeptidase I
-
-
Aminopeptidase III
aminopeptidase IV
-
-
Aminopeptidase yscI
Aminopeptidase yscII
-
-
-
-
Aminopeptidase yscXVI
-
-
-
-
Aminopolypeptidase
-
-
-
-
Amylorhizin aminopeptidase
-
-
-
-
Amylorizin
-
-
-
-
Ape2 aminopeptidase
-
-
API
-
-
-
-
L-aminopeptidase
-
-
-
-
LAPIV
-
-
-
-
Leu.AP
-
-
-
-
Leucin aminopeptidase V
-
-
-
-
Leucine aminopeptidase IV
-
-
-
-
leucine-aminopeptidase
-
-
Leucineaminopeptidase I
-
-
-
-
Metallo aminopeptidase
-
-
-
-
Polypeptidase
-
-
-
-
vacuolar aminopeptidase 1
-
-
vacuolar aminopeptidase I
-
-
Yeast aminopeptidase I
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-94-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala 4-nitroanilide + H2O
Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
Arg 4-nitroanilide + H2O
Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
Cystinyl 4-nitroanilide + H2O
Cystine + 4-nitroaniline
show the reaction diagram
-
-
-
?
Glu 4-nitroanilide + H2O
Glu + 4-nitroaniline
show the reaction diagram
-
-
-
?
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
show the reaction diagram
-
-
-
-
?
L-Ala-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-Gly-Gly ethyl ester + H2O
L-Ala + Gly-Gly ethyl ester
show the reaction diagram
-
-
-
-
?
L-Ala-L-Asp-L-Phe methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Leu + H2O
L-Ala + L-Leu
show the reaction diagram
-
-
-
-
?
L-Ala-L-Thr + H2O
L-Ala + L-Thr
show the reaction diagram
-
-
-
-
?
L-Ala-L-Thr-Gly methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Thr-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-L-Thr-L-Ala methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
show the reaction diagram
-
preferred substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
L-Leu-Gly + H2O
L-Leu + Gly
show the reaction diagram
-
-
-
-
?
L-Leu-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
L-Leu-Gly-L-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
L-Leu-L-Ala + H2O
L-Leu + L-Ala
show the reaction diagram
-
-
-
-
?
L-Leu-L-Leu + H2O
L-Leu + L-Leu
show the reaction diagram
-
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
show the reaction diagram
-
low activity
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
low activity
-
-
?
L-Phe-Gly + H2O
L-Phe + Gly
show the reaction diagram
-
-
-
-
?
L-Phe-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
-
best substrate
-
-
?
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
show the reaction diagram
-
-
-
?
Phe 4-nitroanilide + H2O
Phe + 4-nitroaniline
show the reaction diagram
-
-
-
?
Pro 4-nitroanilide + H2O
Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
S-Benzoyl-Cys 4-nitroanilide + H2O
S-Benzoyl-Cys + 4-nitroaniline
show the reaction diagram
-
-
-
?
Val 4-nitroanilide + H2O
Val + 4-nitroaniline
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Br-
-
activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10 phenanthroline
-
-
2,2'-dipyridyl
-
-
2,3-Dimercaptopropanol
-
-
bestatin
N-(hydroxyethyl)iminodiacetic acid
-
i.e. Himda
nitriloacetic acid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
Ala-Gly-Gly
-
-
3.2
Ala-Thr-Ala
-
-
2.7
Ala-Thr-Ala methyl ester
-
-
0.0225
Cystinyl 4-nitroanilide
-
-
14
L-Ala-Gly-Gly ethyl este
-
-
-
6
L-Ala-L-Th
-
-
-
7
L-Leu-Gly-L-Leu
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33300
Ala-Thr-Ala
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
-
UV-irradiation of cultures increases specific activity
3000
-
substrate Ala-Thr-Ala
980
-
substrate Leu-Gly-Gly
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
absence of activators
7 - 8
-
substrate cystinyl 4-nitroanilide
7 - 8.5
-
presence of Zn2+ and Cl-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
no activity at pH 4 and pH 9, about 33% of maximal activity at pH 6
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
-
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
glycosylated enzyme form
Manually annotated by BRENDA team
-
glycosylated enzyme form
Manually annotated by BRENDA team
additional information
-
Ape2 activity is found in allphases of growth
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
Saccharomyces cerevisiae cells deficient in Lap4 absorb almost 3fold as much cadmium as the wild type strain
physiological function
-
Lap4 is involved in glutathione degradation, under cadmium stress, Lap4 and gamma-glutamyl transferase work together to assure an efficient glutathione turnover stored in the vacuole
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
dimeric form, sucrose density gradient centrifugation
140000
-
glycosylated active enzyme form, gel filtration
320000
-
hexameric form, sucrose density gradient centrifugation
400000
-
beyond 400000 Da, gel filtration
45000
-
x * 45000, SDS-PAGE
50000
-
12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity
51000
-
12 * 51000, SDS-PAGE
52000
-
gel filtration, non-denaturing PAGE
53000
610000
-
sucrose density gradient centrifugation
640000
85000 - 90000
-
unglycosylated active enzyme form, gel filtration
97634
-
1 * 97634, amino acid sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45000, SDS-PAGE
dodecamer
hexamer
homododecamer
-
12 * 50000, the active enzyme is a homododecameric complex of about 600 kDa, and dissociation into two hexamers leads to loss of enzymatic activity
monomer
-
1 * 97634, amino acid sequence calculation
additional information
-
dimeric and hexameric enzyme forms are inactive
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
proteolytic modification
additional information
-
the zymogen is unglycosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 0.1 M Tris-HCl pH 6.5, 30% polyethylene glycol 400, 0.1 M MgCl2 and 1.1 M NaCl
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
4°C, 3 weeks, 10% loss of activity
28298
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl buffer, pH 7.2, 38% loss of activity after 4 days, 81% loss of activity after 11 days
-
frozen, 50 mM ammonium acetate buffer, pH 6.2
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aminopeptidase yscXVI
-
glutathione Sepharose 4B column chromatography, Superdex 200 gel filtration, Superdex 75 gel filtration, and Resource RPC column chromatography
-
isolation of homogeneous dodecameric enzyme
-
native enzyme either 331fold by ammonium sulfate fractionation, heat precipitation, gel filtration, ion exchange and adsorption chromatography, or by a single step anion exchange chromatography process
-
recombinant wild-type and mutant precursor enzymes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
gene APE1, DNA and amino acid sequence determination and analysis, single copy gene, expression of wild-type and mutant precursor enzymes in yeast
-
gene APE1, DNA and amino acid sequence determination and analysis, transcription is regulated by growth phase and by carbon source
-
gene APE2, DNA and amino acid sequence determination and analysis, genetic structure
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klionsky, D.J.
Nonclassical protein sorting to the yeast vacuole
J. Biol. Chem.
273
10807-10810
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Martinez, E.; Jimenez, M.A.; Segui-Real, B.; Vandekerckhove, J.; Sandoval, I.V.
Folding of the presequence of yeast pAPI into an amphipathic helix determines transport of the protein from the cytosol to the vacuole
J. Mol. Biol.
267
1124-1138
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kim, J.; Scott, S.V.; Oda, M.N.; Klionsky, D.J.
Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway
J. Cell Biol.
137
609-618
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Scott, S.V.; Baba, M.; Ohsumi, Y.; Klionsky, D.J.
Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism
J. Cell Biol.
138
37-44
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Oda, M.N.; Scott, S.V.; Hefner-Gravink, A.; Caffarelli, A.C.; Klionsky, D.J.
Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I
J. Cell Biol.
132
999-1010
1996
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Scott, S.V.; Klionsky, D.J.
In vitro reconstitution of cytoplasm to vacuole protein targeting in yeast
J. Cell Biol.
3131
1727-1735
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Segui-Real, B.; Martinez, M.; Sandoval, I.V.
Yeast aminopeptidase I is post-translationally sorted from the cytosol to the vacuole by a mechanism mediated by its bipartite N-terminal extension
EMBO J.
14
5476-5484
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Tisljar, U.; Wolf, D.H.
Purification and characterization of the cystinyl bond cleaving yeast aminopeptidase yscXVI
FEBS Lett.
322
191-196
1993
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hetz, G.; Rhm, K.H.
Interaction of chloride with yeast aminopeptidase I. Equilibrium binding studies
Biol. Chem. Hoppe-Seyler
368
63-66
1987
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rhm., K.H.
Chloride as allosteric effector of yeast aminopeptidase I
Arch. Biochem. Biophys.
239
216-225
1985
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rhm., K.H.
Metal binding to yeast aminopeptidase I
Eur. J. Biochem.
146
633-639
1985
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schwencke, J.; Moustacchi, E.
Proteolytic activities in yeast after UV irradiation. I. Variation in proteinase levels in repair proficient Rad+ strains
Mol. Gen. Genet.
185
290-295
1982
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lffler, H.G.; Rhm.K.H.
Comparative studies on the dodecameric and hexameric forms of yeast aminopeptidase I
Z. Naturforsch. C
34
381-386
1979
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Metz, G.; Marx, R.; Rhm, K.H.
The quarternary structure of yeast aminopeptidase I 1. Molecular forms and subunit size
Z. Naturforsch. C
32
929-937
1977
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Metz, G.; Rhm.K.H.
Yeast aminopeptidase I. Chemical composition and catalytic properties
Biochim. Biophys. Acta
429
933-949
1976
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Cueva, R.; Garcia-Alvarez, N.; Suarez-Rendueles, P.
Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene
FEBS Lett.
259
125-129
1989
Saccharomyces cerevisiae (P14904), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Caprioglio, D.R.
Yeast aminopeptidases Ape2, Aap1' and Yin7
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
316-318
2004
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Suarez-Rendueles, P.; Bordallo, J.; Cueva, R.
Aminopeptidase I
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
940-941
2004
Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Andrei-Selmer, C.; Knuppel, A.; Satyanarayana, C.; Heese, C.; Schu, P.V.
A new class of mutants deficient in dodecamerization of aminopeptidase 1 and vacuolar transport
J. Biol. Chem.
276
11606-11614
2001
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Adachi, W.; Suzuki, N.N.; Fujioka, Y.; Suzuki, K.; Ohsumi, Y.; Inagaki, F.
Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathway
Acta Crystallogr. Sect. F
63
200-203
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Schu, P.
Aminopeptidase I enzymatic activity
Methods Enzymol.
451
67-78
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Adamis, P.; Mannarino, S.; Riger, C.; Duarte, G.; Cruz, A.; Pereira, M.; Eleutherio, E.
Lap4, a vacuolar aminopeptidase I, is involved in cadmium-glutathione metabolism
Biometals
22
243-249
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team