Information on EC 3.4.11.10 - bacterial leucyl aminopeptidase

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

EC NUMBER
COMMENTARY hide
3.4.11.10
-
RECOMMENDED NAME
GeneOntology No.
bacterial leucyl aminopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
show the reaction diagram
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
37288-67-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene BB0069
SwissProt
Manually annotated by BRENDA team
strain SR3
-
-
Manually annotated by BRENDA team
strain SR3
-
-
Manually annotated by BRENDA team
LAP preferentially localizes inside the epithelial cells that line the alimentary tract of the adult worm
-
-
Manually annotated by BRENDA team
strain CCRC 11223
-
-
Manually annotated by BRENDA team
strain 47b
-
-
Manually annotated by BRENDA team
strain 47b
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
single copy gene
SwissProt
Manually annotated by BRENDA team
strain ATCC 35404
-
-
Manually annotated by BRENDA team
gene pepA or Xoo0834
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
immunization with recombinant Fasciola gigantica LAP (FgLAP) elicits high levels of immune responses and protection against Fasciola gigantica in mice
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Gly + H2O
Ala + Gly
show the reaction diagram
-
-
-
ir
albomycin + H2O
?
show the reaction diagram
Arg-Phe + H2O
Arg + Phe
show the reaction diagram
-
-
-
ir
casein + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
Cys-Gly + H2O
Cys + Gly
show the reaction diagram
Cys-Gly + H2O
L-Cys + Gly
show the reaction diagram
-
preferred substrate
-
-
?
DL-Ala-Gly-Gly + H2O
DL-Ala + Gly-Gly
show the reaction diagram
-
-
-
ir
DL-Leu-Gly-DL-Phe + H2O
DL-Leu + Gly-DL-Phe
show the reaction diagram
-
-
-
ir
DL-Leu-Gly-Gly + H2O
DL-Leu + Gly-Gly
show the reaction diagram
-
-
-
ir
Glu-Phe + H2O
Glu + Phe
show the reaction diagram
-
-
-
ir
glutathione + H2O
?
show the reaction diagram
-
the enzyme is involved in turnover of glutathione
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gly
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
Gly-7-amido-4-methylcoumarin + H2O
Gly + 7-amino-4-methylcoumarin
show the reaction diagram
-
very weak activity
-
-
?
Ile-amide + H2O
Ile + NH3
show the reaction diagram
-
-
-
ir
Ile-Phe + H2O
Ile + Phe
show the reaction diagram
-
-
-
ir
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
low activity
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Ala-L-Ala-L-Phe
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
show the reaction diagram
-
1% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
show the reaction diagram
-
3% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Asp
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
very weak activity
-
-
?
L-Cys-4-nitroanilide + H2O
L-Cys + 4-nitroaniline
show the reaction diagram
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-cystinyl-p-nitroanilide + H2O
L-cystine + p-nitroaniline
show the reaction diagram
-
10% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Gln-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Gln
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Glu-7-amido-4-methylcoumarin + H2O
L-Glu + 7-amino-4-methylcoumarin
show the reaction diagram
-
very weak activity
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
show the reaction diagram
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
L-Leu-Gly-Gly + H2O
L-Leu + Gly-Gly
show the reaction diagram
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
show the reaction diagram
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
L-leucine anilide + H2O
L-leucine + aniline
show the reaction diagram
-
-
-
?
L-leucine ethyl ester + H2O
L-leucine + ethanol
show the reaction diagram
-
-
-
?
L-leucine-4-anisidide + H2O
L-leucine + anisidine
show the reaction diagram
-
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
L-leucine-p-nitroanilide + H2O
L-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
L-leucyl-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-leucyl-L-leucyl-L-leucine + H2O
L-leucine + L-leucyl-L-leucine
show the reaction diagram
-
-
-
-
?
L-Lys-4-nitroanilide + H2O
4-nitroaniline + L-Lys
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-p-nitroanilide + H2O
L-Lys + p-nitroaniline
show the reaction diagram
-
24% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Met
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Phe-p-nitroanilide + H2O
L-Phe + p-nitroaniline
show the reaction diagram
-
23% activity compared to L-Leu-p-nitroanilide
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Pro
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Pro-7-amido-4-methylcoumarin + H2O
L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Thr
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Thr-7-amido-4-methylcoumarin + H2O
L-Thr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Trp
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Tyr
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
show the reaction diagram
low activity
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
show the reaction diagram
-
very weak activity
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + beta-nitroaniline
show the reaction diagram
Leu-Ala + H2O
Leu + Ala
show the reaction diagram
Leu-amide + H2O
Leu + NH3
show the reaction diagram
Leu-Arg + H2O
Leu + Arg
show the reaction diagram
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
show the reaction diagram
Leu-Gly + H2O
Leu + Gly
show the reaction diagram
-
-
-
ir
Leu-Ile + H2O
Leu + Ile
show the reaction diagram
Leu-Leu + H2O
Leu + Leu
show the reaction diagram
Leu-Met + H2O
Leu + Met
show the reaction diagram
Leu-methyl ester + H2O
Leu + methanol
show the reaction diagram
-
-
-
ir
Leu-Phe + H2O
Leu + Phe
show the reaction diagram
Leu-Trp + H2O
Leu + Trp
show the reaction diagram
Leu-Tyr + H2O
Leu + Tyr
show the reaction diagram
Leu-Val + H2O
Leu + Val
show the reaction diagram
leucine-4-nitroaniline + H2O
?
show the reaction diagram
-
enzyme also shows activity towards Arg-4-nitroaniline, Lys-4-nitroaniline and Met-4-nitroaniline
-
-
?
Lys-Gly + H2O
Lys + Gly
show the reaction diagram
-
-
-
ir
Met-amide + H2O
Met + NH3
show the reaction diagram
-
-
-
ir
Met-beta-naphthylamide + H2O
Met + beta-naphthylamine
show the reaction diagram
-
-
-
ir
Met-Leu-4-nitroanilide + H2O
Met-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Met-Leu-7-amido-4-methylcoumarin + H2O
Met-Leu + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Met-Phe + H2O
Met + Phe
show the reaction diagram
-
-
-
ir
norleucinamide + H2O
norleucine + NH3
show the reaction diagram
oxidized insulin B chain + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37°C
-
-
?
peptides + H2O
N-terminal amino acid + peptide(n-1)
show the reaction diagram
-
-
-
?
Phe-amide + H2O
Phe + NH3
show the reaction diagram
-
-
-
ir
Phe-Asp-Ser-Ala-Val + H2O
Phe + Asp-Ser-Ala-Val
show the reaction diagram
-
-
-
ir
Phe-beta-naphthylamide + H2O
Phe + beta-naphthylamine
show the reaction diagram
Phe-Gly + H2O
Phe + Gly
show the reaction diagram
-
-
-
ir
Phe-methyl ester + H2O
Phe + methanol
show the reaction diagram
-
-
-
ir
Phe-Phe + H2O
Phe + Phe
show the reaction diagram
-
-
-
ir
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
show the reaction diagram
-
-
-
ir
Pro-Phe-Pro + H2O
Pro + Phe-Pro
show the reaction diagram
-
-
-
ir
recombinant human methionine-interferon alpha-2b + H2O
L-methionine + recombinant human interferon alpha-2b
show the reaction diagram
-
-
-
-
?
thionoleucine-4-anisidide + H2O
thionoleucine + anisidine
show the reaction diagram
-
-
-
?
thionoleucine-S-anilide + H2O
thionoleucine + aniline
show the reaction diagram
-
-
-
?
Thr-beta-naphthylamide + H2O
Thr + beta-naphthylamine
show the reaction diagram
-
3.3% of rate of hydrolysis of Leu-beta-naphthylamide
-
ir
Tyr-Gly + H2O
Tyr + Gly
show the reaction diagram
-
-
-
ir
Val-amide + H2O
Val + NH3
show the reaction diagram
-
-
-
ir
Val-beta-naphthylamide + H2O
Val + beta-naphthylamine
show the reaction diagram
-
-
-
ir
Val-Gly + H2O
Val + Gly
show the reaction diagram
-
-
-
ir
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
albomycin + H2O
?
show the reaction diagram
-
PepA activates albomycin
-
-
?
Cys-Gly + H2O
Cys + Gly
show the reaction diagram
-
glutathione-derived substrate, PepA is involved in the cysteine salvage pathway
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
inhibits activity; weakly inhibits activity
K+
slightly activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,2-Cyclohexanedione
-
Ki: 0.022-0.023 mM
1-aminoindan-2-one
-
-
1-Butaneboronate
1-butaneboronic acid
1-Phenyl-2-thiourea
-
; competitive
2,3-Butanedione
-
photochemical inactivation: effect only in the light, proportional to light intensity, modification of 5 Trp-, 3-4 Tyr-, 2 His- and 2Arg-residues, no photoinactivation in the absence of oxygen or in the presence of azide, protection also by Trp, Met, D-Met, L-2-thiol-His, 2-mercaptoethanol, Gly-Met, Ki: 5.1-19.8 mM
2,3-Pentanedione
-
photochemical inactivation: effect only in UV-light
2-amino-1,4-dihydro-2-isoquinolin-3-one
-
-
2-aminocycloheptanone
-
-
2-hydroxy-1,4-dihydro-2H-isoquinolin-3-one
-
-
2-mercaptoethanol
-
-
2-methylquinolin-8-ol
-
-
2-propanol
-
Ki: 8 mM
3-amino-1,2,3,4-tetrahydronaphthalene-2-carbohydroxamic acid
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-ethanone
-
-
3-amino-1,2,3,4-tetrahydronaphthalene-2-phosphonic acid
-
-
3-amino-2-tetralone
-
-
3-amino-3,4-dihydro-1H-naphtalen-2-one
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(2-phenylethyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(3-phenylpropyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(4-phenylbutyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(5-phenylpentyl)oxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-benzyloxime
-
-
3-amino-3,4-dihydro-1H-naphthalen-2-one O-methyloxime
-
-
3-methyl-1,2-cyclopentanedione
-
Ki: 0.48-1.19 mM
3-methyl-1-butanol
-
Ki: 0.98 mM
3-methylquinolin-8-ol
-
-
4-iodo-D-phenylalanine hydroxamate
5,7-dibromoquinolin-8-ol
-
-
5,7-dichloroquinolin-8-ol
-
-
5,7-diiodoquinolin-8-ol
-
-
5-(trifluoromethyl)quinolin-8-ol
-
-
5-bromo-2-methylquinolin-8-ol
-
-
5-bromo-8-hydroxy-2-methylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,2-dimethylquinoline-7-sulfonamide
-
-
5-bromo-8-hydroxy-N,N,2-trimethylquinoline-7-sulfonamide
-
-
5-bromoquinolin-8-ol
-
-
5-chloro-2-methylquinolin-8-ol
-
-
5-chloro-7-iodoquinolin-8-ol
-
-
5-chloro-8-hydroxy-N,N-dimethylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxy-N-methylquinoline-7-sulfonamide
-
-
5-chloro-8-hydroxyquinoline-7-sulfonamide
-
-
5-chloroquinolin-8-ol
-
-
5-fluoroquinolin-8-ol
-
-
5-iodoquinolin-8-ol
-
-
5-nitroquinolin-8-ol
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one
-
-
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-oxime
-
-
8-hydroxy-N,N-dimethylquinoline-5-sulfonamide
-
-
amastatin
-
reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1
Amino acid hydroxamates
-
-
aminoquinolinone
-
-
Aprotinin
-
the recombinant enzyme shows 58.9% relative activity in the presence of 0.001 mM aprotinin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
benzyl alcohol
-
Ki: 2.6 mM
bestatin
cysteine
D-Leu-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Leu-hydroxamate
-
Ki: 2 nM, L-isomer bound 150 times less tightly
D-Val-4-nitroanilide
-
D-isomers of the substrates inhibit the enzyme
D-Val-hydroxamate
-
Ki: 5 nM
dithiothreitol
DL-Ala-hydroxamate
-
Ki: 0.0055 mM
DL-dithiothreitol
-
-
DL-Phe-hydroxamate
-
Ki: 0.0008 mM
DL-Thr-hydroxamate
-
Ki: 0.002 mM
DL-Val-hydroxamate
-
Ki: 10 nM
E-64
-
the recombinant enzyme shows 43% relative activity in the presence of 0.005 mM E-64 on hydrolysis of L-Leu-7-amido-4-methylcoumarin
epibestatin
-
Ki: 0.07 mM
ethanol
-
Ki: 80 mM
Glyoxal
-
Ki: 3.7-6.5 mM
H2O2
-
the enzyme is sensitive against oxidative damage by H2O2
isothiochroman-3-one
-
-
L-Ala-hydroxamate
-
Ki: 0.02 mM
L-cysteine
-
strongly inhibited by cysteine
L-leucine
-
competitive inhibition
L-leucine 4-nitroanilide
-
-
L-leucine anilide
-
-
L-leucine anisidide
-
-
L-leucine phosphonic acid
L-leucinephosphonic acid
-
competitive, interacts with both metal ions in the dinuclear active site, inhibition mechanism
L-leucinethiol
L-Leucinol
-
competitive
L-Phe-hydroxamate
-
Ki: 0.0088 mM
L-Thr-hydroxamate
-
Ki: 0.066 mM
L-Val-hydroxamate
-
Ki: 0.0022 mM
Leu-bromomethyl ketone
Leu-chloromethyl ketone
-
reversible, Ki: 670 nM; succinimido derivative, reversible, Ki: 0.17 mM
Leu-methyl ketone
leucine phosphonic acid
-
competitive inhibition
leupeptin
-
the recombinant enzyme shows 32.7% relative activity in the presence of 0.01 mM leupeptin on hydrolysis of L-Leu-7-amido-4-methylcoumarin
methanol
-
Ki: 860 mM
methylglyoxal
-
photochemical inactivation: effect only in UV-light, Ki: 1.8-2.0 mM
N-alpha-tosyl-L-lysine chlormethyl ketone
-
the recombinant enzyme shows 28.9% relative activity in the presence of 0.005 mM N-alpha-tosyl-L-lysine chlormethyl ketone on hydrolysis of L-Leu-7-amido-4-methylcoumarin
n-butanol
-
Ki: 2.7 mM
N-mercapto-leucyl-4-nitroanilides
-
-
N-mercaptoacyl-leucyl-p-nitroaniline
-
synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition, Ki: 2.5-57 nM
-
n-Propanol
-
Ki: 11 mM
n-valeramide
Na2S
-
60% loss of activity at 10 mM
p-iodo-D-Phe hydroxamate
-
structure of enzyme-inhibitor complex: Glu151 has crucial functional role
-
Pepstatin
-
-
pepstatin A
-
the recombinant enzyme shows 26.1% relative activity in the presence of 1 mM pepstatin A on hydrolysis of L-Leu-7-amido-4-methylcoumarin
phenol
-
Ki: 4 mM
Phenylglyoxal
phenylmethylsulfonyl fluoride
-
the recombinant enzyme shows 24.5% relative activity in the presence of 1 mM phenylmethylsulfonyl fluoride on hydrolysis of L-Leu-7-amido-4-methylcoumarin
Phenylurea
-
-
Propylene glycol
-
-
quinolin-8-ol
-
-
t-butyloxycarbonyl-L-Leu
-
bromomethyl ketone derivative, utilized for purification procedure
-
tert-butanol
-
Ki: 10 mM
Thioglycollate
-
60% loss of activity at 10 mM
thionoleucine-S-anilide
-
-
thionoleucine-S-anisidide
-
-
Tris
-
buffer inhibition; chelated to active site Zn2+
Urea
-
competitive
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
activates, 30% activation at 17 mM
bicarbonate
-
activates
dithiothreitol
-
activates, 23% activation at 0.021 mM, inhibition above
additional information
-
full-length LAP is activated in a two-step process: proteolytic cleavage at the C terminus is followed by an intramolecular autocatalytic removal of a 12-amino acid propeptide at the N terminus
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
Arg-Phe
-
-
0.39 - 0.48
Cys-Gly
0.14
Gly-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
1
Ile-amide
-
-
0.03
Ile-Phe
-
-
10
L-Ala-4-nitroanilide
pH 8.0, 30°C
0.231
L-Ala-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.26
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
-
pH 8.0, 37°C
0.6
L-Arg-4-nitroanilide
pH 8.0, 30°C
0.078
L-Arg-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
1 - 7.51
L-Arg-p-nitroanilide
0.077
L-Cys-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.056 - 0.11
L-cystinyl-p-nitroanilide
0.01 - 4.4
L-Leu-4-nitroanilide
0.038 - 0.18
L-Leu-7-amido-4-methylcoumarin
25
L-Leu-Gly-Gly
-
pH 7.6-7.8, 60°C
0.57 - 1.79
L-Leu-p-nitroanilide
0.01 - 15
L-leucine 4-nitroanilide
45 - 78
L-leucine anilide
0.7
L-leucine ethyl ester
-
-
32 - 50
L-leucine-4-anisidide
0.22 - 0.85
L-Lys-4-nitroanilide
0.093 - 0.24
L-Met-7-amido-4-methylcoumarin
0.066
L-Phe-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
0.06
L-Thr-7-amido-4-methylcoumarin
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1 mM MnCl2, at 37°C
19
L-Val-4-nitroanilide
pH 8.0, 30°C
5.1
Leu-amide
-
-
0.39
Leu-Arg
-
-
0.1 - 0.43
Leu-beta-naphthylamide
0.38
Leu-Ile
-
-
0.18
Leu-Leu
-
-
0.35
Leu-Met
-
-
8.5
Leu-methyl ester
-
-
0.05 - 0.86
Leu-Phe
0.96
Leu-Trp
-
-
1.5
Leu-Tyr
-
-
0.64
Leu-Val
-
-
0.97
leucine-4-nitroaniline
-
pH 8.5, 60°C
-
14.6
Met-amide
-
-
0.96
Met-beta-naphthylamide
-
-
1.1
Met-Phe
-
-
6.3
norleucinamide
-
-
10.8
norvalinamide
-
-
1.8
Phe-amide
-
-
0.52
Phe-beta-naphthylamide
-
-
3.9
Phe-methyl ester
-
-
2.1
Phe-Phe
-
-
0.02726
recombinant human methionine-interferon alpha-2b
-
pH 6.0, 37°C
-
4 - 7
thionoleucine-4-anisidide
4 - 11
thionoleucine-S-anilide
2.4
Val-amide
-
-
0.19
Val-beta-naphthylamide
-
-
0.07
Val-Phe
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
Arg-Phe
Aeromonas caviae
-
-
43.3 - 60
Cys-Gly
0.001
Glu-Phe
Aeromonas caviae
-
-
11
Gly-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
6.2
Ile-amide
Vibrio proteolyticus
-
-
10
Ile-Phe
Aeromonas caviae
-
-
0.37
L-Ala-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30°C
192000
L-Ala-7-amido-4-methylcoumarin
Fasciola hepatica
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
10
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
34
L-Arg-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30°C
59900
L-Arg-7-amido-4-methylcoumarin
Fasciola hepatica
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
1.26 - 82
L-Arg-p-nitroanilide
288100
L-Cys-7-amido-4-methylcoumarin
Fasciola hepatica
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
3.71 - 46.7
L-cystinyl-p-nitroanilide
0.017 - 10180
L-Leu-4-nitroanilide
17 - 246000
L-Leu-7-amido-4-methylcoumarin
49540
L-Leu-Gly-Gly
Geobacillus thermoleovorans
-
pH 7.6-7.8, 60°C
30 - 128
L-Leu-p-nitroanilide
1.1 - 4320
L-leucine 4-nitroanilide
6.3 - 16
L-leucine anilide
96
L-leucine ethyl ester
Vibrio proteolyticus
-
-
3.8 - 9.5
L-leucine-4-anisidide
10 - 17.7
L-Lys-4-nitroanilide
20 - 283200
L-Met-7-amido-4-methylcoumarin
33800
L-Phe-7-amido-4-methylcoumarin
Fasciola hepatica
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
16200
L-Thr-7-amido-4-methylcoumarin
Fasciola hepatica
-
recombinant enzyme, in 0.1 M glycine buffer, pH 8.5 containing 1mM MnCl2, at 37°C
0.43
L-Val-4-nitroanilide
Bacillus subtilis
P25152
pH 8.0, 30°C
15
Leu-Ala
Vibrio proteolyticus
-
-
220
Leu-amide
Vibrio proteolyticus
-
-
39
Leu-Arg
Vibrio proteolyticus
-
-
29.6 - 38
Leu-beta-naphthylamide
16
Leu-Ile
Vibrio proteolyticus
-
-
8.3
Leu-Leu
Vibrio proteolyticus
-
-
53
Leu-Met
Vibrio proteolyticus
-
-
145
Leu-methyl ester
Vibrio proteolyticus
-
-
41 - 72
Leu-Phe
58
Leu-Trp
Vibrio proteolyticus
-
-
85
Leu-Tyr
Vibrio proteolyticus
-
-
15
Leu-Val
Vibrio proteolyticus
-
-
32
Met-amide
Vibrio proteolyticus
-
-
8.2
Met-beta-naphthylamide
Aeromonas caviae
-
-
22
Met-Phe
Aeromonas caviae
-
-
60
norleucinamide
Vibrio proteolyticus
-
-
67
norvalinamide
Vibrio proteolyticus
-
-
67
peptide
Vibrio proteolyticus
-
-
6.2
Phe-amide
Vibrio proteolyticus
-
-
6.3
Phe-beta-naphthylamide
Aeromonas caviae
-
-
42
Phe-methyl ester
Vibrio proteolyticus
-
-
158
Phe-Phe
Aeromonas caviae
-
-
0.000853
recombinant human methionine-interferon alpha-2b
Vibrio proteolyticus
-
pH 6.0, 37°C
-
7.5 - 12.2
thionoleucine-4-anisidide
7.7 - 23.3
thionoleucine-S-anilide
6.5
Val-amide
Vibrio proteolyticus
-
-
0.26
Val-beta-naphthylamide
Aeromonas caviae
-
-
1.3
Val-Phe
Aeromonas caviae
-
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
68
Gly-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
8818
34
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
10236
91
L-Leu-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
3540
82
L-Lys-4-nitroanilide
Escherichia coli
-
pH 8.0, 37°C
3734
81
L-Met-7-amido-4-methylcoumarin
Escherichia coli
-
pH 8.0, 37°C
3910
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 0.023
1,2-Cyclohexanedione
-
-
0.0027
1-Butaneboronate
0.24
1-Phenyl-2-thiourea
-
pH 8.0, 25°C
5.1 - 19.8
2,3-Butanedione
-
photochemical inactivation: effect only in the light, proportional to light intensity, modification of 5 Trp-, 3-4 Tyr-, 2 His- and 2Arg-residues, no photoinactivation in the absence of oxygen or in the presence of azide, protection also by Trp, Met, D-Met, L-2-thiol-His, 2-mercaptoethanol, Gly-Met
0.004
2-hydroxy-1,4-dihydro-2H-isoquinolin-3-one
-
-
0.1
2-methylquinolin-8-ol
-
value above, pH 8, 25°C
8
2-propanol
-
-
0.004
3-amino-1,2,3,4-tetrahydronaphthalene-2-carbohydroxamic acid
-
-
0.48 - 1.19
3-methyl-1,2-cyclopentanedione
-
-
0.98
3-methyl-1-butanol
-
-
0.00046
3-methylquinolin-8-ol
-
pH 8, 25°C
0.1
5,7-dibromoquinolin-8-ol
-
value above, pH 8, 25°C
0.1
5,7-dichloroquinolin-8-ol
-
value above, pH 8, 25°C
0.1
5,7-diiodoquinolin-8-ol
-
value above, pH 8, 25°C
0.00037
5-(trifluoromethyl)quinolin-8-ol
-
pH 8, 25°C
0.1
5-bromo-2-methylquinolin-8-ol
-
value above, pH 8, 25°C
0.1
5-bromo-8-hydroxy-2-methylquinoline-7-sulfonamide
-
value above, pH 8, 25°C
0.1
5-bromo-8-hydroxy-N,2-dimethylquinoline-7-sulfonamide
-
value above, pH 8, 25°C
0.1
5-bromo-8-hydroxy-N,N,2-trimethylquinoline-7-sulfonamide
-
value above, pH 8, 25°C
0.016
5-bromoquinolin-8-ol
-
pH 8, 25°C
0.1
5-chloro-2-methylquinolin-8-ol
-
value above, pH 8, 25°C
0.1
5-chloro-7-iodoquinolin-8-ol
-
value above, pH 8, 25°C
0.1
5-chloro-8-hydroxy-N,N-dimethylquinoline-7-sulfonamide
-
value above, pH 8, 25°C
0.00081
5-chloro-8-hydroxy-N-methylquinoline-7-sulfonamide
-
pH 8, 25°C
0.00019
5-chloro-8-hydroxyquinoline-7-sulfonamide
-
pH 8, 25°C
0.011
5-chloroquinolin-8-ol
-
pH 8, 25°C
0.00068
5-fluoroquinolin-8-ol
-
pH 8, 25°C
0.000062
5-iodoquinolin-8-ol
-
pH 8, 25°C
0.029
5-nitroquinolin-8-ol
-
pH 8, 25°C
0.1
8-hydroxy-N,N-dimethylquinoline-5-sulfonamide
-
value above, pH 8, 25°C
0.000058
amastatin
-
reversible, slow, tight binding, transition state analog complex, stoichiometry of inhibition 1:1
0.08
aminoquinolinone
-
-
2.6
benzyl alcohol
-
-
0.000001
bestatin
-
recombinant enzyme, at 37°C
0.000002
D-Leu-hydroxamate
-
L-isomer bound 150 times less tightly
0.000005
D-Val-hydroxamate
-
-
0.0055
DL-Ala-hydroxamate
-
-
0.0008
DL-Phe-hydroxamate
-
-
0.002
DL-Thr-hydroxamate
-
-
0.00001
DL-Val-hydroxamate
-
-
0.07
epibestatin
-
-
80
ethanol
-
-
3.7 - 6.5
Glyoxal
-
-
0.004
isothiochroman-3-one
-
-
0.02
L-Ala-hydroxamate
-
-
0.000025
L-cysteine
-
recombinant enzyme, at 37°C
0.0019
L-leucine
-
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
0.0055
L-leucine 4-nitroanilide
-
enzyme with 2 Co2+ or Zn2+ bound, pH 8.0, 25°C
0.0066
L-leucinephosphonic acid
-
metal free enzyme, pH 8.0, 25°C
0.000007
L-leucinethiol
-
-
0.017
L-Leucinol
-
-
0.0088
L-Phe-hydroxamate
-
-
0.0022
L-Thr-hydroxamate
-
-
860
L-Val-hydroxamate
-
-
0.0002
Leu-bromomethyl ketone
0.00067 - 0.17
Leu-chloromethyl ketone
0.0019
leucine phosphonic acid
-
wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C
1.8 - 2
methylglyoxal
-
photochemical inactivation: effect only in UV-light
2.7
n-butanol
-
-
0.0000025 - 0.000057
N-mercapto-leucyl-4-nitroanilides
-
-
0.0000025 - 0.000057
N-mercaptoacyl-leucyl-p-nitroaniline
-
synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition
-
11
n-Propanol
-
-
0.002 - 0.0023
Phenylglyoxal
-
-
0.00058
quinolin-8-ol
-
pH 8, 25°C
10
tert-butanol
-
-
4.6
Urea
-
pH 8.0, 25°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
1-aminoindan-2-one
Vibrio proteolyticus
-
pH 7.5, 25°C
0.74
2-amino-1,4-dihydro-2-isoquinolin-3-one
Vibrio proteolyticus
-
-
0.35
2-aminocycloheptanone
Vibrio proteolyticus
-
pH 7.5, 25°C
0.5
3-amino-1,2,3,4-tetrahydronaphthalene-2-ethanone
Vibrio proteolyticus
-
-
0.15
3-amino-1,2,3,4-tetrahydronaphthalene-2-phosphonic acid
Vibrio proteolyticus
-
-
0.13
3-amino-2-tetralone
Vibrio proteolyticus
-
-
0.13
3-amino-3,4-dihydro-1H-naphtalen-2-one
Vibrio proteolyticus
-
pH 7.5, 25°C
0.17
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(2-phenylethyl)oxime
Vibrio proteolyticus
-
-
0.3
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(3-phenylpropyl)oxime
Vibrio proteolyticus
-
-
0.11
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(4-phenylbutyl)oxime
Vibrio proteolyticus
-
-
0.13
3-amino-3,4-dihydro-1H-naphthalen-2-one O-(5-phenylpentyl)oxime
Vibrio proteolyticus
-
-
0.21
3-amino-3,4-dihydro-1H-naphthalen-2-one O-benzyloxime
Vibrio proteolyticus
-
-
0.8
3-amino-3,4-dihydro-1H-naphthalen-2-one O-methyloxime
Vibrio proteolyticus
-
-
0.9
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one
Vibrio proteolyticus
-
pH 7.5, 25°C
0.015
7-amino-5,7,8,9-tetrahydrobenzocyclohepten-6-oxime
Vibrio proteolyticus
-
pH 7.5, 25°C
0.0000016
bestatin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
-
recombinant enzyme, using L-Glu-7-amido-4-methylcoumarin as substrate, at 37°C
0.0002
-
native enzyme, using L-Glu-7-amido-4-methylcoumarin as substrate, at 37°C
0.0003
-
native enzyme, using L-Asp-7-amido-4-methylcoumarin as substrate, at 37°C
0.0005
-
native enzyme, using Gly-7-amido-4-methylcoumarin as substrate, at 37°C
0.0006
-
native enzyme, using L-Val-7-amido-4-methylcoumarin as substrate, at 37°C
0.001
purified enzyme
0.0012
-
recombinant enzyme, using L-Asp-7-amido-4-methylcoumarin as substrate, at 37°C
0.0019
-
native enzyme, using L-Ser-7-amido-4-methylcoumarin as substrate, at 37°C; recombinant enzyme, using Gly-7-amido-4-methylcoumarin as substrate, at 37°C
0.0021
-
recombinant enzyme, using L-Ser-7-amido-4-methylcoumarin as substrate, at 37°C
0.0025
-
recombinant enzyme, using L-Val-7-amido-4-methylcoumarin as substrate, at 37°C
0.003
-
supernatant clarification, in 10 mM Tricine buffer, pH 8.0, at 25°C
0.0032
-
native enzyme, using L-Pro-7-amido-4-methylcoumarin as substrate, at 37°C
0.0054
-
native enzyme, using L-Tyr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0056
-
recombinant enzyme, using L-Pro-7-amido-4-methylcoumarin as substrate, at 37°C
0.0062
-
recombinant enzyme, using L-Ile-7-amido-4-methylcoumarin as substrate, at 37°C
0.0064
-
recombinant enzyme, using L-Tyr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0068
-
recombinant enzyme, using L-Phe-7-amido-4-methylcoumarin as substrate, at 37°C
0.0075
-
recombinant enzyme, using L-Ala-7-amido-4-methylcoumarin as substrate, at 37°C
0.0083
-
native enzyme, using L-Ala-7-amido-4-methylcoumarin as substrate, at 37°C
0.0093
-
native enzyme, using L-Ile-7-amido-4-methylcoumarin as substrate, at 37°C
0.0141
-
native enzyme, using L-Phe-7-amido-4-methylcoumarin as substrate, at 37°C
0.0253
-
recombinant enzyme, using L-Met-7-amido-4-methylcoumarin as substrate, at 37°C
0.0291
-
recombinant enzyme, using L-Arg-7-amido-4-methylcoumarin as substrate, at 37°C
0.0355
-
recombinant enzyme, using L-Thr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0657
-
native enzyme, using L-Met-7-amido-4-methylcoumarin as substrate, at 37°C
0.0694
-
native enzyme, using L-Thr-7-amido-4-methylcoumarin as substrate, at 37°C
0.0752
-
native enzyme, using L-Arg-7-amido-4-methylcoumarin as substrate, at 37°C
0.0831
-
recombinant enzyme, using L-Cys-7-amido-4-methylcoumarin as substrate, at 37°C
0.0953
-
native enzyme, using L-Cys-7-amido-4-methylcoumarin as substrate, at 37°C
0.1344
-
native enzyme, using L-Leu-7-amido-4-methylcoumarin as substrate, at 37°C
0.2145
-
recombinant enzyme, using L-Leu-7-amido-4-methylcoumarin as substrate, at 37°C
1.67
-
value about, substrate L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin; value about, substrate L-Asp-7-amido-4-methylcoumarin; value about, substrate L-Gln-7-amido-4-methylcoumarin; value about, substrate L-Thr-7-amido-4-methylcoumarin; value about, substrate L-Trp-7-amido-4-methylcoumarin
3
-
azo-enzyme
4.17
-
value about, substrate L-Pro-7-amido-4-methylcoumarin
8.3
-
value about, substrate L-Tyr-7-amido-4-methylcoumarin
10.41
-
free recombinant wild-type enzyme
13.8
-
mutant enzyme D380E, at 60°C, using L-Leu-4-nitroanilide as substrate
15.1
-
mutant enzyme D380V, at 60°C, using L-Leu-4-nitroanilide as substrate
15.86
-
immobilized recombinant wild-type enzyme
16
-
substrate L-leucine-4-nitroanilidepH 8.0, 37°C
17
-
nitro-enzyme
18.22
-
free recombinant Lys9-tagged enzyme
20
-
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treated enzyme
21.71
-
free recombinant Lys3-tagged enzyme
22
-
mutant enzyme D198M/F221W, using L-Leu-p-nitroanilide as a substrate
25
-
value about, substrate Gly-7-amido-4-methylcoumarin
33.3
-
value about, substrate L-Leu-7-amido-4-methylcoumarin; value about, substrate L-Lys-4-nitroanilide; value about, substrate L-Met-7-amido-4-methylcoumarin
34.5
-
mutant enzyme Y532L, at 60°C, using L-Leu-4-nitroanilide as substrate
55.3
-
mutant enzyme D380N, at 60°C, using L-Leu-4-nitroanilide as substrate
60.73
-
immobilized recombinant Lys3-tagged enzyme
60.8
purified recombinant mutant H227L
64
purified recombinant enzyme
68
-
wild type enzyme, using L-Leu-p-nitroanilide as a substrate
76.91
-
immobilized recombinant Lys9-tagged enzyme
80 - 115
-
native enzyme, buffer dependent
84
-
diethylpyrocarbonate-treated enzyme
91.3
purified recombinant mutant H191L
91.6
-
purified recombinant wild-type enzyme
104.9
-
mutant enzyme Y532D, at 60°C, using L-Leu-4-nitroanilide as substrate
133.4
purified recombinant wild-type enzyme
466.7
-
purified recombinant enzyme
572.5
-
wild type enzyme, at 60°C, using L-Leu-4-nitroanilide as substrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
the activity of CGase for Cys-Gly is optimum at pH 7.3
7.5 - 8.5
-
assay at
7.5 - 9.5
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10.5
-
activity range, profiles of free and immobilized recombinant wild-type and mutant enzymes, overview
5.5 - 10
-
pH profile, about 40% of maximal activity at pH 5.5 and pH 10.0, rapid decline of activity at pH 5.0, recombinant enzyme
5.5 - 10.8
-
pH-profile of mutant E151H
6 - 9
20% of maximal activity at pH 6.0, 50% at pH 9.0
7 - 9
-
optimal activity is observed at pH 8-8.5, exhibiting a rapid decline under mildly acidic (below pH 7) and basic (above pH 9) conditions
additional information
the enzyme is inactive at low pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
assay at
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 100
-
temperature profile, about 60% of maximal activity at 15°C and 100°C, recombinant enzyme
30 - 70
-
activity range, profiles of free and immobilized recombinant wild-type and mutant enzymes, overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expressed in the cecal epithelial cells of adult parasites as shown by in situ hybridisation
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)