Information on EC 3.4.13.19 - membrane dipeptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.13.19
-
RECOMMENDED NAME
GeneOntology No.
membrane dipeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of dipeptides
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gliotoxin biosynthesis
-
-
leukotriene biosynthesis
-
-
arachidonic acid metabolism
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-99-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BORI
-
-
Manually annotated by BRENDA team
strain BORI
-
-
Manually annotated by BRENDA team
strains DSM 15814T, CD76, CR20, CF51, CI35, and CM17
-
-
Manually annotated by BRENDA team
strain DSM20451
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-
Manually annotated by BRENDA team
strain DSM20451
-
-
Manually annotated by BRENDA team
-
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
glutathione metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-2-methylpropanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2R)-2-amino-3-phenylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-2-methylpropanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]propanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-biphenyl-4-ylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]-4-methylpentanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-cyclohexylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-2-amino-3-naphthalen-2-ylpropanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(dimethylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(formylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
(2S,3S)-2-[[(2S)-3-cyclohexyl-2-(methylamino)propanoyl]amino]-3-[([1-[(2R,4S,5R)-4-hydroxy-5-(hydroxymethyl)-3-methylidenetetrahydrofuran-2-yl]-2-oxo-1,2-dihydropyrimidin-4-yl]carbamoyl)oxy]butanoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala + H2O
Ala + Ala
show the reaction diagram
Ala-Gln + H2O
Ala + Gln
show the reaction diagram
-
100% activity
-
-
?
Ala-Gly + H2O
Ala + Gly
show the reaction diagram
Ala-Leu + H2O
Ala + Leu
show the reaction diagram
-
14.0% activity compared to Ala-Gln
-
-
?
Ala-Met + H2O
Ala + Met
show the reaction diagram
-
-
-
-
?
Ala-Phe + H2O
Ala + Phe
show the reaction diagram
Arg-Phe + H2O
Arg + Phe
show the reaction diagram
-
6.3% activity compared to Ala-Gln
-
-
?
Asp-Phe + H2O
Asp + Phe
show the reaction diagram
-
4.9% activity compared to Ala-Gln
-
-
?
B-type natriuretic peptide 1-32 + H2O
B-type natriuretic peptide 3-32 + ?
show the reaction diagram
-
-
-
-
?
beta-lactam + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ala-D-Ala + H2O
D-Ala + D-Ala
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
D-Ala-L-Ala + H2O
D-Ala + L-Ala
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
gamma-L-glutamyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Ala + H2O
Gly + Ala
show the reaction diagram
-
L-Ala and D-Ala
-
-
?
Gly-D-Leu + H2O
Gly + D-Leu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
Gly-D-Phe + H2O
Gly + D-Phe
show the reaction diagram
Gly-Gly + H2O
Gly + Gly
show the reaction diagram
Gly-Leu + H2O
Gly + Leu
show the reaction diagram
Gly-Phe + H2O
Gly + Phe
show the reaction diagram
-
-
-
-
?
Gly-Trp + H2O
Gly + Trp
show the reaction diagram
-
-
-
-
?
Gly-Val + H2O
Gly + Val
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
L-Ala-D-Ala + H2O
L-Ala + D-Ala
show the reaction diagram
-
assay at 30°C, pH 7.5
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-
?
L-Ala-Gly + H2O
L-Ala + Gly
show the reaction diagram
L-Ala-L-Ala + H2O
L-Ala + L-Ala
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-Arg + H2O
L-Ala + L-Arg
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-Asp + H2O
L-Ala + L-Asp
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-Gln + H2O
L-Ala + L-Gln
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-Glu + H2O
L-Ala + L-Glu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-His + H2O
L-Ala + L-His
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ala-L-Lys + H2O
L-Ala + L-Lys
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Arg-D-Asp + H2O
L-Arg + D-Asp
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Arg-Gly + H2O
L-Arg + Gly
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Arg-L-Asp + H2O
L-Arg + L-Asp
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Asn-D-Glu + H2O
L-Asn + D-Glu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Cys-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
L-cysteinylglycine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystinyl-bis-glycine + H2O
?
show the reaction diagram
L-Leu-D-Ala + H2O
L-Leu + D-Ala
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Leu-D-Glu + H2O
L-Leu + D-Glu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Leu-D-Leu + H2O
L-Leu + D-Leu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Leu-D-Ser + H2O
L-Leu + D-Ser
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Leu-L-Asp + H2O
L-Leu + L-Asp
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Leu-L-Leu + H2O
L-Leu + L-Leu
show the reaction diagram
L-Met-D-Glu + H2O
L-Met + D-Glu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Met-D-Leu + H2O
L-Met + D-Leu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Met-L-Leu + H2O
L-Met + L-Leu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
L-Ser-Gly + H2O
L-Ser + Gly
show the reaction diagram
-
-
-
-
?
L-Tyr-D-Leu + H2O
L-Tyr + D-Leu
show the reaction diagram
-
assay at 30°C, pH 7.5
-
-
?
Leu-Gly + H2O
Leu + Gly
show the reaction diagram
Leu-Leu + H2O
Leu + Leu
show the reaction diagram
Leu-Phe + H2O
Leu + Phe
show the reaction diagram
-
12.5% activity compared to Ala-Gln
-
-
?
Leu-Trp + H2O
Leu + Trp
show the reaction diagram
-
10.2% activity compared to Ala-Gln
-
-
?
leukotriene D4 + H2O
?
show the reaction diagram
leukotriene D4 + H2O
leukotriene E4
show the reaction diagram
-
-
-
?
Lys-Gly + H2O
Lys + Gly
show the reaction diagram
-
-
-
-
?
Met-Met + H2O
Met + Met
show the reaction diagram
N-acylated carbapenems + H2O
?
show the reaction diagram
N-formimidoyl thienamycin + H2O
?
show the reaction diagram
-
-
-
-
?
N-formimidoyl thienamycin derivative MK0787 + H2O
?
show the reaction diagram
N-[([(1S,2R)-2-[(3-cyclohexyl-L-alanyl)amino]-3-hydroxy-1-methylpropyl]oxy)carbonyl]-2'-deoxy-2'-methylidenecytidine + H2O
?
show the reaction diagram
-
-
-
-
?
N-[([(1S,2S)-2-[(3-cyclohexyl-L-alanyl)amino]-1,4-dimethyl-3-oxopentyl]oxy)carbonyl]-2'-deoxy-2'-methylidenecytidine + H2O
?
show the reaction diagram
-
-
-
-
?
nonbasic N-acylated thienamycin + H2O
?
show the reaction diagram
Phe-Ala + H2O
Phe + Ala
show the reaction diagram
-
6.7% activity compared to Ala-Gln
-
-
?
Phe-Gly + H2O
Phe + Gly
show the reaction diagram
Phe-Tyr + H2O
Phe + Tyr
show the reaction diagram
-
-
-
-
?
pro-B-type natriuretic peptide 1-108 + H2O
pro-B-type natriuretic peptide 3-108 + ?
show the reaction diagram
-
-
-
-
?
S-1-menaphthyl-L-Cys-Gly + H2O
S-1-menaphthyl-L-Cys + Gly
show the reaction diagram
-
-
-
-
?
S-2,4-dinitrophenyl-L-Cys-Gly + H2O
2,4-dinitrophenol + L-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-4-nitrobenzyl-L-Cys-Gly + H2O
4-nitrobenzyl alcohol + L-Cys-Gly
show the reaction diagram
-
-
-
-
?
S-N-ethylmaleimide-L-cysteinyl-glycine + H2O
?
show the reaction diagram
-
-
-
-
?
thienamycin + H2O
?
show the reaction diagram
Trp-Gly + H2O
Trp + Gly
show the reaction diagram
-
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
show the reaction diagram
-
9.5% activity compared to Ala-Gln
-
-
?
Tyr-Phe + H2O
Tyr + Phe
show the reaction diagram
-
3.8% activity compared to Ala-Gln
-
-
?
Val-Gly + H2O
Val + Gly
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
leukotriene D4 + H2O
?
show the reaction diagram
-
the enzyme is involved in the reanal metabolism of glutathione and its conjugates such as leukotriene
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-(trifluoromethyl)phenyl)acrylic acid
-
50% inhibition at 10 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-bromophenyl)acrylic acid
-
50% inhibition at 6 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-fluorophenyl)acrylic acid
-
50% inhibition at 5 nM
(2Z)-2-[[(1-amino-2-cyclohexylethyl)(hydroxy)phosphoryl]methyl]-3-(4-iodophenyl)acrylic acid
-
50% inhibition at 8 nM
1,10-phenanthroline
acetate
-
-
bestatin
Cd2+
-
-
Cilastatin
CN-
-
-
Co2+
-
-
cysteine
-
-
Cystinyl-bis-glycine
-
inhibition above 0.2 mM, substrate below
Dansylethylenediamine
-
cilastatin protects
guanosine triphosphate
-
-
HCO3-
-
-
L-Cys-Gly
-
substrate inhibition
N-bromosuccinimide
-
-
N-Ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline
-
cilastatin protects
N-ethylmaleimide
-
22% inhibition at 1 mM
Ni2+
-
-
NO3-
-
-
nucleotides
-
-
-
p-hydroxymercuribenzoate
-
-
Phenylmethylsulfonylfluoride
-
41% inhibition at 1 mM
phosphate
-
-
phosphinate mimic of L-Ala-D-Asp
-
-
Pro-Ala
-
competitive to hydrolysis of Gly-Leu
SO42-
-
-
thiol compounds
-
-
Z-2-(2,2-Dimethylcyclopropanecarboxamido)-2-butenoic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Insulin
-
stimulates indirectly the release of RDPase in association with Ca2+ in a concentration-dependent manner (half maximal release at 0.58 nM)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.111
beta-lactam
-
membrane-bound dipeptidase-1
0.65
Cystinyl-bis-glycine
-
-
0.77 - 12.5
Gly-D-Phe
1.22
Gly-L-Leu
-
-
0.99
Gly-L-Phe
-
-
2.03
Gly-L-Trp
-
-
11
Gly-L-Val
-
-
0.79
Gly-Leu
-
-
0.102 - 1
glycyldehydrophenylalanine
4.4
L-Ala-D-Ala
-
pH 7.5, 30°C
0.8
L-Ala-Gly
-
-
13.8
L-Ala-L-Asp
-
pH 7.5, 30°C
16
L-Ala-L-Gln
-
pH 7.5, 30°C
9.5
L-Ala-L-Glu
-
pH 7.5, 30°C
0.14
L-Arg-D-Asp
-
-
1.8 - 8.8
L-Arg-L-Asp
2.4
L-Asn-D-Glu
-
pH 7.5, 30°C
1.51
L-cysteinylglycine
-
-
0.45 - 2.5
L-cystinyl-bis-Gly
0.75
L-Leu-D-Ala
-
-
0.55
L-Leu-D-Glu
-
pH 7.5, 30°C
0.37
L-Leu-D-Leu
-
pH 7.5, 30°C
2
L-Leu-D-Ser
-
pH 7.5, 30°C
0.21
L-Leu-Gly
-
-
2
L-Leu-L-Asp
-
pH 7.5, 30°C
0.056 - 1.4
L-Leu-L-Leu
0.89
L-Met-D-Glu
-
pH 7.5, 30°C
0.56
L-Met-D-Leu
-
pH 7.5, 30°C
2.3
L-Met-L-Leu
-
pH 7.5, 30°C
0.67
L-Phe-Gly
-
-
0.15
L-Trp-Gly
-
-
0.17
L-Tyr-D-Leu
-
pH 7.5, 30°C
0.09
L-Val-Gly
-
-
0.005 - 0.01
leukotriene D4
0.0025
S-1-menaphthyl-L-Cys-Gly
-
pH 7.0, 37°C
2.9
S-2,4-dinitrophenyl-L-Cys-Gly
-
pH 7.0, 37°C
0.67
S-4-nitrobenzyl-L-Cys-Gly
-
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
750
L-Ala-D-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
1400
L-Ala-L-Asp
Streptomyces coelicolor
-
pH 7.5, 30°C
140
L-Ala-L-Gln
Streptomyces coelicolor
-
pH 7.5, 30°C
220
L-Ala-L-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
107
L-Arg-D-Asp
Streptomyces coelicolor
-
-
0.4 - 132
L-Arg-L-Asp
288
L-Asn-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
160
L-Leu-D-Ala
Streptomyces coelicolor
-
-
135
L-Leu-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
21
L-Leu-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
400
L-Leu-D-Ser
Streptomyces coelicolor
-
pH 7.5, 30°C
160
L-Leu-L-Asp
Streptomyces coelicolor
-
pH 7.5, 30°C
140
L-Leu-L-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
340
L-Met-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
194
L-Met-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
310
L-Met-L-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
24
L-Tyr-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
additional information
L-Arg-L-Asp
Streptomyces coelicolor
-
mutant D22H, value below 0.03, pH 7.5, 30°C; mutant D320A, value below 0.03, pH 7.5, 30°C; mutant D320N, value below 0.03, pH 7.5, 30°C; mutant R223M, value below 0.03, pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
D-Ala-D-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
1348
0.0022
D-Ala-L-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
15691
33
Gly-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
44168
170
L-Ala-D-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
9194
14
L-Ala-L-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
2849
0.18
L-Ala-L-Arg
Streptomyces coelicolor
-
pH 7.5, 30°C
44294
100
L-Ala-L-Asp
Streptomyces coelicolor
-
pH 7.5, 30°C
40523
8.4
L-Ala-L-Gln
Streptomyces coelicolor
-
pH 7.5, 30°C
40525
24
L-Ala-L-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
40524
0.45
L-Ala-L-His
Streptomyces coelicolor
-
pH 7.5, 30°C
100787
0.072
L-Ala-L-Lys
Streptomyces coelicolor
-
pH 7.5, 30°C
160395
760
L-Arg-D-Asp
Streptomyces coelicolor
-
pH 7.5, 30°C
40516
22
L-Arg-Gly
Streptomyces coelicolor
-
pH 7.5, 30°C
160394
0.046 - 72
L-Arg-L-Asp
5167
120
L-Asn-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
40522
210
L-Leu-D-Ala
Streptomyces coelicolor
-
pH 7.5, 30°C
40515
250
L-Leu-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
40519
56
L-Leu-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
20337
200
L-Leu-D-Ser
Streptomyces coelicolor
-
pH 7.5, 30°C
40520
83
L-Leu-L-Asp
Streptomyces coelicolor
-
pH 7.5, 30°C
34423
100
L-Leu-L-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
9199
380
L-Met-D-Glu
Streptomyces coelicolor
-
pH 7.5, 30°C
40517
350
L-Met-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
40518
140
L-Met-L-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
34422
150
L-Tyr-D-Leu
Streptomyces coelicolor
-
pH 7.5, 30°C
40521
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
L-Cys-Gly
-
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.44
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
glycyldehydrophenylalanine
9 - 11
-
enzyme form S
9
-
enzyme form F
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
enzyme form S
70
-
enzyme form F
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 4.8
-
-
4.89
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
of animals orally exposed to different doses of cadmium for one month. Activity of enzyme as well as carboxypeptidase A and Na+/K+ ATPase in the mucosa of the proximal end of the small intestine are dose-dependently reduced after exposure. In the distal small intestine, enzyme activities are almost restored
Manually annotated by BRENDA team
-
expression of membrane-bound dipeptidase-3 is not detectable, weak expression of membrane-bound dipeptidase-1 and membrane-bound dipeptidase-2
Manually annotated by BRENDA team
-
expression of membrane-bound dipeptidase-3 is not detectable, weak expression of membrane-bound dipeptidase-1 and membrane-bound dipeptidase-2
Manually annotated by BRENDA team
-
expression of membrane-bound dipeptidase-1 and membrane-bound dipeptidase-3 is not detectable, weak activity of membrane-bound dipeptidase-2
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
2 * 45000, SDS-PAGE under reducing conditions (MW 80000 Da: SDS-PAGE under nonreducing conditions)
47200
-
approach to equilibrium measurement
48600
-
2 * 48600, electrophoresis under reducing conditions
49000
-
native enzyme, SDS-PAGE
49500
-
2 * 49500, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
53333
-
6 * 53333, gel filtration
55000
-
6 * 55000, SDS-PAGE
62000
-
2 * 62000, SDS-PAGE under reducing conditions
64680
-
LTQ mass spectrometry
66000
-
2 * 66000, enzyme form F, SDS-PAGE
87000 - 93000
-
sedimentation equilibrium measurement, gel filtration
92510
-
MALDI-TOF
94000 - 96000
-
gel filtration
94000
-
1 * 94000 + 1 * 115000, enzyme form S, SDS-PAGE
95300
-
sedimentation equilibrium analysis
100000
105000
-
gel filtration
115000
-
1 * 94000 + 1 * 115000, enzyme form S, SDS-PAGE
130000
-
SDS-PAGE under nonreducing conditions
135000
-
enzyme form F, gel filtration
180000
-
gel filtration
200000
-
enzyme form S, gel filtration
218000
-
gel filtration
220000
-
HPLC gel filtration
320000
-
gel filtration
330000
-
SDS-PAGE
additional information
-
primary structure
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 47000, SDS-PAGE
homohexamer
-
6 * 53333, gel filtration; 6 * 55000, SDS-PAGE
tetramer
-
4 * 59000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
additional information
-
not a glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
very low activity (less than about 10%) is observed below pH 5.5, at pH 10.0 the activity is about 50% of the maximum, the enzyme is stable for 30 min over the pH range 4.0 to 8.0
677698
5
-
inactivation below
647088
6
-
unstable below, both enzyme forms
647108
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
the enzyme shows about 30% and 50% of the maximum activity at 20°C and 70°C, respectively, stable at temperatures up to 70°C, but the activity decreased rapidly above 80°C
40
-
enzyme form S is unstable above
53
-
12 min, about 50% loss of activity
60
-
enzyme form F is stable up to
70
-
30 min, about 15% loss of activity of the native enzyme, about 55% of the activity of the Co2+-reconstituted enzyme, about 75% loss of activity of the Mn2+-reconstituted enzyme
additional information
-
substitution of Co2+ or Mn2+ for Zn2+ considerably lowers the thermostability of the enzyme without affecting the overall conformation of the protein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extended dialysis against nonchelating buffers does not result in loss of activity
-
no loss of activity upon lyophilization
-
substitution of Co2+ or Mn2+ for Zn2+ considerably lowers the thermostability of the enzyme without affecting the overall conformation of the protein
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10% (v/v) glycerol, few days, activity is greatly diminished
-
-80°C, 10% (v/v) glycerol, few days, activity is greatly diminished
-
4°C, 10% (v/v) glycerol, few days, remains stable
-
4°C, sterile filtration, stable for 1 year
-
frozen, in dilute solution, 0.13 mg/ml Tris-HCl buffer, pH 8, loses two-third of its activity after 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 forms different in electrophoretic mobility: form S (slow) and F (fast)
-
affinity purification of enzyme solubilized with detergent
-
ammonium sulfate precipitation, size exclusion chromatography, ion exchange chromatography and gel filtration
-
partial
-
recombinant enzyme is purified by nickel-chelating affinity chromatography, wild type enzyme is purified by ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Q-Sepharose column chromatography
-
Sephadex G-25 gel filtration, Toyopearl Butyl-650M column chromatography, Toyopearl DEAE-650M column chromatography, and Sephacryl S-200 gel filtration
-
ultracentrifugation and Superose 12 (10/300) gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) Codon Plus-RIL cells
-
expressed in Mus musculus
expression in Cos-1 cells
-
expression in Escherichia coli BL21
-
expression of membrane-bound dipeptidase-2 and membrane-bound dipeptidase-3 in COS cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H413K/H417K
-
catalytic activity reduced to background levels. Animals carrying the mutant enzyme generate 1 embryo from 22 plugged females compared to 153 embryos from 19 females in wild-type. There is no difference in sperm count, morphology or motility after capacitation in mutant animals. While sperm from wild-type males readily binds to the zona pellucida of unfertilized eggs, sperm from homozygous mutant males shows background levels of binding
D22H
-
mutant with no residual enzyme acitvity
D320A
-
mutant with no residual enzyme acitvity
D320N
-
mutant with no residual enzyme acitvity
H150A
-
mutant with more than doubled Km-values
H150N
-
mutant with more than doubled Km-values
R223K
-
mutant with about 3fold reduced activity compared to wild-type enzyme
R223M
-
mutant with no residual enzyme acitvity
H128L
-
mutant enzyme exhibits a specific activity and Km for Gly-D-Phe comparable with that of the wild-type enzyme
H152L
-
inactive mutant enzyme is expressed at the cell surface at equivalent levels to the wild-type, the mutant enzyme fails to bind to cilastatin-Sepharose in contrast to the wild-type enzyme
H198K
-
inactive mutant enzyme is expressed at the cell surface at equivalent levels to the wild-type
H20L
-
inactive mutant enzyme is expressed at the cell surface at equivalent levels to the wild-type
H49K
-
mutant enzyme exhibits a specific activity and Km for Gly-D-Phe comparable with that of the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in 20 mM Tris-HCl, pH 8.0, 500 mM arginine, containing 1 mM reduced glutathione, 0.2 mM oxidized glutathione, and sodium chloride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
dicarboxypeptidase activity of testis angiotensin-converting enzyme is required for fertility. Animals carrying mutant enzyme without catalytic activity generate 1 embryo from 22 plugged females compared to 153 embryos from 19 females in wild-type
nutrition
-
cadmium given in drinking water compromises protein digestion and absorption of nutrients particularly in the proximal region of small intestine
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