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Information on EC 3.4.24.B6 - matrix metalloproteinase-20 and Organism(s) Bos taurus and UniProt Accession O18767

for references in articles please use BRENDA:EC3.4.24.B6
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B6 matrix metalloproteinase-20
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This record set is specific for:
Bos taurus
UNIPROT: O18767
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
proteolytic degradation of ameloblastin
proteolytic cleavage of ameloblastin
Synonyms
mmp20, mmp-20, enamelysin, matrix metalloproteinase-20, matrix metalloproteinase 20, enamel protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enamel metalloproteinase
-
enamelysin
-
M10.019
Merops-ID
enamelysin
-
-
matrix metalloproteinase 20
-
-
MMP-20
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
CAS REGISTRY NUMBER
COMMENTARY hide
185766-51-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amelogenin + H2O
?
show the reaction diagram
cleavage loci: FSY/EVL, GGW/LHH, MFP/MQP, MLP/DLT, LTL/EAW, AWP/STD
-
-
?
amylogenin + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
-
-
?
leucine-rich amylogenin peptide + H2O
leucine-rich amylogenin residues 181-186 + leucine-rich amylogenin residues 187-188
show the reaction diagram
corresponds to residues 181-188 of amylogenin, recombinant enzyme, cleavage site is P186-A187
-
?
Mca-PLGL-Dpa-AR + H2O
?
show the reaction diagram
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
-
-
?
tyrosine-rich amylogenin peptide + H2O
tyrosine-rich amylogenin residues 36-45 + tyrosine-rich amylogenin residues 46-49
show the reaction diagram
corresponds to residues 36-49 of amylogenin, recombinant enzyme, cleavage site is W45-L46
-
?
amelogenin + H2O
?
show the reaction diagram
-
-
-
-
?
amylogenin + H2O
?
show the reaction diagram
-
-
-
?
Mca-PLGL-Dpa-AR + H2O
?
show the reaction diagram
-
-
-
-
?
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2 + H2O
?
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
amylogenin + H2O
?
show the reaction diagram
involved in tooth formation
-
?
proteins + H2O
peptides
show the reaction diagram
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
neither calcium nor magnesium alone can effectively activate the proenzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0143
Mca-PLGL-Dpa-AR
37°C
0.0143
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2
at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9
Mca-PLGL-Dpa-AR
37°C
9
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2
at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at, zymography with casein at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
secretion
Manually annotated by BRENDA team
fetal tooth tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
in enamel matrix of teeth
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP20_BOVIN
481
0
53781
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 55000, SDS-PAGE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
sequential autolysis, activation of recombinant proform by urea
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the addition of 1 mM EDTA into activation buffer can protect the 55 kDa proenzyme from autolysis and degradation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged pro-enzyme from Escherichia coli
Ni-NTA column chromatography
-
nickel resin chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression of His-atgged pro-enzyme in Escherichia coli BL21(DE3)
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation from inclusion bodies after overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, W.; Machule, D.; Gao, C.; DenBesten, P.K.
Activation of recombinant bovine matrix metalloproteinase-20 and its hydrolysis of two amelogenin oligopeptides
Eur. J. Oral Sci.
107
352-359
1999
Bos taurus (O18767), Bos taurus
Manually annotated by BRENDA team
Wang, S.; Zhu, J.; Zhang, Y.; Li, L.; DenBesten, P.; Li, W.
On-column activation of bovine recombinant metalloproteinase 20
Anal. Biochem.
356
291-293
2006
Bos taurus
Manually annotated by BRENDA team
Zhu, L.; Tanimoto, K.; Robinsin, S.; Chen, J.; Witkowska, E.; Hall, S.; Le, T.; Denbesten, P.K.; Li, W.
Comparative properties of recombinant human and bovine matrix metalloproteinase-20
Arch. Oral Biol.
53
785-790
2008
Bos taurus, Bos taurus (O18767), Homo sapiens, Homo sapiens (O60882)
Manually annotated by BRENDA team