Any feedback?
Information on EC 3.4.21.82 - Glutamyl endopeptidase II
for references in articles please use BRENDA:EC3.4.21.82Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.82 Glutamyl endopeptidase IISpecify your search results
Word Map
- 3.4.21.82
- proteinases
-
diisopropyl
- fluorophosphate
- casein
- aureus
-
glu-specific
- intermedius
- licheniformis
- p-nitroanilide
- alcalase
- endopeptidases
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
glusgp, glutamyl proteinase, glutamic acid-specific protease, glutamyl endopeptidase 2, bl-gse, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GluSGP
-
-
-
-
Glutamic acid-specific protease
-
-
-
-
glutamyl endopeptidase 2
SGPE
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: -Glu-/- >> -Asp-/-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-/-Asp- and -Glu-/-Pro- bonds is slow
preferential cleavage:-Glu-+- >>-Asp-+-. Preference for Pro or Leu at P2 and Phe at P3. Cleavage of-Glu-+-Asp and-Glu-+-Pro- bonds is slow, the term-+- depicts the point of cleavage
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
137010-42-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2-Aminobenzoyl-Ala-Ala-Glu-Val-Tyr(NO2)-Asp-OH + H2O
2-Aminobenzoyl-Ala-Ala-Glu + Val-Tyr(NO2)-Asp-OH
-
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Gly-Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Ile-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Leu-Ala-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Leu-GLy-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Met-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-2-carboxyphenyl thioester + Nva-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Gly-Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Ile-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Leu-Ala-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Leu-Gly-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Met-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-3-carboxyphenyl ester + Nva-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Gly-Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Ile-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Leu-Ala-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Leu-Gly-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Leu-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Met-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-4-carboxyphenyl ester + Nva-NH2
?
-
-
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Gly-Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Ile-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Leu-Ala-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Leu-Gly-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Met-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxyethyl thioester + Nva-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Gly-Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Ile-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Leu-Ala-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Leu-Gly-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Met-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Ala-carboxymethyl thioester + Nva-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Gly-Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Ile-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Leu-Ala-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Leu-Gly-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Met-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Asp-methyl ester + Nva-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Gly-Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Ile-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Leu-Ala-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Leu-Gly-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Met-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl ester + Nva-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Gly-Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Ile-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Leu-Ala-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Leu-Gly-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Leu-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Met-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
benzyloxycarbonyl-Glu-methyl thioester + Nva-NH2
?
-
protease catalyzed acyltransfer from substrates to amino acid amides
-
?
Benzyloxycarbonyl-Leu-Leu-Glu 2-naphthylamide + H2O
Benzyloxycarbonyl-Leu-Leu-Glu + 2-naphthylamine
-
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Glu 2-nitroanilide + H2O
Benzyloxycarbonyl-Phe-Leu-Glu + 4-nitroaniline
-
-
-
-
?
Synthetic peptide substrates containing an N-terminal anthraniloyl group and a 3-nitrotyrosine close to the C-terminus + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Ala-Ala-Pro-Asp 4-nitroanilide + H2O
tert-butoxycarbonyl-Ala-Ala-Pro-Asp + 4-nitroaniline
-
slowly
-
-
?
tert-butoxycarbonyl-Ala-Ala-Pro-Glu 4-nitroanilide + H2O
tert-butoxycarbonyl-Ala-Ala-Pro-Glu + 4-nitroaniline
-
-
-
-
?
tert-butoxycarbonyl-Ala-Phe-Pro-Glu 4-nitroanilide + H2O
tert-butoxycarbonyl-Ala-Phe-Pro-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-Ala-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Ala-Ala-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-Gly-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Ala-Gly-Glu + 4-nitroaniline
-
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Leu-Glu-4-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Leu-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-Phe-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Ala-Phe-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-Pro-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Ala-Pro-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Leu-Pro-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Leu-Pro-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Phe-Pro-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Phe-Pro-Glu + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Pro-Glu 4-nitroanilide + H2O
Tert-Butyloxycarbonyl-Ala-Pro-Glu + 4-nitroaniline
-
-
-
-
?
benzlyoxycarbonyl-Ala-Ala-Met-Glu-p-nitroanilide + H2O
?
-
-
-
?
benzlyoxycarbonyl-Ala-Ala-Trp-Glu-p-nitroanilide + H2O
?
-
-
-
?
insulin + H2O
?
-
hydrolyzes Glu4-Gln5, Glu17-Asp18, and Cys11-Ser12 bonds in the oxidized A-chain of insulin and Glu13-Ala14, Glu21-Arg22, Cys7-Gly8, and Cys19-Gly20 bonds in the oxidized B-chain of insulin
-
?
insulin + H2O
?
-
hydrolyzes Glu4-Gln5, Glu17-Asp18, and Cys11-Ser12 bonds in the oxidized A-chain of insulin and Glu13-Ala14, Glu21-Arg22, Cys7-Gly8, and Cys19-Gly20 bonds in the oxidized B-chain of insulin
-
?
additional information
?
-
-
does not hydrolyze the subtilisin substrate benzyloxycarbonyl-Ala-Ala-Leu-p-nitroanilide, only little activity with benzyloxycarbonyl-Ala-Ala-Trp-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Leu-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Phe-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Met-Asp-p-nitroanilide, and benzyloxycarbonyl-Gly-Ala-Ala-Asp-p-nitroanilide
-
?
additional information
?
-
-
does not hydrolyze the subtilisin substrate benzyloxycarbonyl-Ala-Ala-Leu-p-nitroanilide, only little activity with benzyloxycarbonyl-Ala-Ala-Trp-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Leu-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Phe-Asp-p-nitroanilide, benzyloxycarbonyl-Ala-Ala-Met-Asp-p-nitroanilide, and benzyloxycarbonyl-Gly-Ala-Ala-Asp-p-nitroanilide
-
?
additional information
?
-
-
preferentially hydrolyzes peptide bonds on the carbonyl-terminal side of either glutamic acid or aspartic acid
-
-
?
additional information
?
-
-
preference for aspartic acid at P4, preference for Ala and Val at P3, preference for Pro and Val at P2, proline is disfavored at P3, P1', and P2' and aspartic acid is disfavored at P1'
-
-
?
additional information
?
-
-
the enzyme favors Pro and Leu residues at S2, while S3 subsite prefers Phe over either Ala or Leu
-
-
?
additional information
?
-
-
hydrolyzes Glu-Xaa bonds approximately 100-fold faster than Asp-Xaa bonds
-
-
?
additional information
?
-
-
binding site comprises at least 6 subsites
-
-
?
additional information
?
-
-
pronounced preference for Glu-Xaa bonds versus Asp-Xaa bonds
-
-
?
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chloromethane analogs of glutamic and aspartic acid-containing substrates
-
-
-
additional information
-
little or no inhibition with PMSF, EDTA, benzamidine, p-CMB, duck ovomucoid, inhibitor from marine anemone, and soybean trypsin inhibitor
-
additional information
-
metal chelators; metals including Hg2+; not: EDTA; SH-blocking agents
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
-
1 * 22000, Streptomyces griseus, SDS-PAGE in presence of 2-mercaptoethanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
1 * 22000, Streptomyces griseus, SDS-PAGE in presence of 2-mercaptoethanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 37
-
without Ca2+, stable at 37°C, but activity decreases at 50°C and 55°C by 55% and 90% respectively
37 - 55
-
with Ca2+, highly thermostable, heating at 37°C, 50°C, and 55°C has no effect on activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
peptide coupling catalyzed by proteasesis an alternative to chemical solution and solid phase peptide synthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, N.; Tsuruyama, S.; Nagata, K.; Hirayama, K.; Noda, K.; Makisumi, S.
Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)
J. Biochem.
104
451-456
1988
Streptomyces griseus
brenda
Nagata, K.; Yoshida, N.; Ogata, F.; Araki, M.; Noda, K.
Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8
J. Biochem.
110
859-862
1991
Streptomyces griseus
brenda
Komiyama, T.; Bigler, T.L.; Yoshida, N.; Noda, K.; Laskowski, M.
Replacement of P1 Leu18 by Glu18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus proteinase (GluSGP)
J. Biol. Chem.
266
10727-10730
1991
Streptomyces griseus
brenda
Breddam, K.; Meldal, M.
Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching
Eur. J. Biochem.
206
103-107
1992
Streptomyces griseus
brenda
Svendsen, I.; Jensen, M.R.; Breddam, K.
The primary structure of the glutamic acid-specific protease of Streptomyces griseus
FEBS Lett.
292
165-167
1991
Streptomyces griseus
brenda
Birktoft, J.J.; Breddam, K.
Glutamyl endopeptidases
Methods Enzymol.
244
114-126
1994
Streptomyces griseus
brenda
Balaban, N.P.; Mardanova, A.M.; Sharipova, M.R.; Gabdrakhmanova, L.A.; Sokolova, E.A.; Garusov, A.V.; Milgotina, E.I.; Rudenskaya, G.N.; Leshchinskaya, I.B.
Isolation and characterization of glutamyl endopeptidase 2 from Bacillus intermedius 3-19
Biochemistry (Moscow)
68
1217-1224
2003
Bacillus intermedius, Bacillus intermedius Mrz 19
brenda
Wehofsky, N.; Wissmann, J.D.; Alisch, M.; Bordusa, F.
Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: design, synthesis, and application
Biochim. Biophys. Acta
1479
114-122
2000
Bacillus licheniformis
brenda
De Leo, F.; Volpicella, M.; Sciancalepore, M.; Gallerani, R.; Ceci, L.R.
One of the three proteinase inhibitor genes newly identified in the Brassica napus genome codes for an inhibitor of glutamyl endopeptidase
FEBS Lett.
580
948-954
2006
Streptomyces griseus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.21.82)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
