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Information on EC 3.4.24.B6 - matrix metalloproteinase-20 and Organism(s) Homo sapiens

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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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
matrix metalloproteinase 20
-
-
MMP-20
MMP20
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of ameloblastin
show the reaction diagram
MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts into the enamel matrix of developing teeth. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. The principle functions of MMP-20 in dental enamel formation is to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins
proteolytic degradation of ameloblastin
show the reaction diagram
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
aggrecan + H2O
?
show the reaction diagram
cleavage site is Asn341-Phe342
-
?
amelogenin + H2O
23 kDa amelogenin + 5 kDa tyrosine-rich amelogenin peptide
show the reaction diagram
cleaves amelogenin between Trp45 and Leu46
-
-
?
amelogenin + H2O
?
show the reaction diagram
amelogenin + H2O
amelogenin fragments rH163 + rH146
show the reaction diagram
-
in high phosphates conditions (20.9 mM KH2PO4) no cleavage site is observed in the central region of residues Q54–P146, which also shows the slowest cleavage rate with the maximum accumulation of fragment rH163 at 4 h time-point. In the no calcium and phosphates conditions, the accumulation of rH163 reaches the maximum amount at 1 h and the cleavage in the central region Q54-P146 appears only after 5 h. Under high calcium conditions (33.4 mM CaCl2), the fastest cleavage rate is observed and also few exclusive and additional cleavage sites at T61, H67. Other conditions also show some exclusive cleavage sites such as P2 for no calcium and phosphates, P50 for low calcium and phosphates and G10 for high calcium and phosphates. The N-terminal positions Y11, N13, F14, S15, E17, K23, W24, P33, G42, and S53 and the C-terminal positions P155 and T158 are cleaved in all conditions used
-
?
amelogenin + H2O
fragments of amelogenin
show the reaction diagram
-
-
-
-
?
amylogenin + H2O
4 major peptide fragments of MWs 24 kDa, 23 kDa, 22 kDa, and 20 kDa
show the reaction diagram
-
-
?
amylogenin + H2O
?
show the reaction diagram
cartilage oligomeric matrix protein + H2O
60 kDa protein
show the reaction diagram
100 kDa protein substrate
-
?
enamel protein + H2O
?
show the reaction diagram
MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts into the enamel matrix of developing teeth. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. The principle functions of MMP-20 in dental enamel formation is to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins
-
-
?
endostatin + H2O
peptides
show the reaction diagram
-
comparison of efficiency to several other proteinases
-
?
Mca-KPLGL-Dpa-AR-NH2 + H2O
?
show the reaction diagram
-
-
-
?
Mca-PLA-norvaline-Dpa-AR-NH2 + H2O
?
show the reaction diagram
synthetic fluorogenic substrate
-
?
Mca-PLGL-Dpa-AR + H2O
?
show the reaction diagram
-
-
-
?
Mca-PLGL-Dpa-AR-NH2 + H2O
?
show the reaction diagram
synthetic fluorogenic substrate
-
?
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2 + H2O
?
show the reaction diagram
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
type V collagen + 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
aggrecan + H2O
?
show the reaction diagram
cleavage site is Asn341-Phe342
-
?
amelogenin + H2O
?
show the reaction diagram
amelogenin with a proline 41 to threonine mutation is hydrolyzed at a lower rate by matrix metalloproteinase 20 (MMP20), resulting in an inherited tooth enamel defect, amelogenesis
-
-
?
amelogenin + H2O
fragments of amelogenin
show the reaction diagram
-
-
-
-
?
amylogenin + H2O
?
show the reaction diagram
involved in tooth formation
-
?
cartilage oligomeric matrix protein + H2O
60 kDa protein
show the reaction diagram
100 kDa protein substrate
-
?
enamel protein + H2O
?
show the reaction diagram
MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts into the enamel matrix of developing teeth. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. The principle functions of MMP-20 in dental enamel formation is to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins
-
-
?
proteins + H2O
peptides
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
NaF
-
0.01 mM NaF downregulates the synthesis of MMP-20 by 21%
SYGYEPMGGWLHHQ
competive against Mca-KPLGL-Dpa-AR-NH2
SYGYETMGGWLHHQ
competive against Mca-KPLGL-Dpa-AR-NH2
tissue matrix metalloprotease inhibitor TIMP-2
complete inhibition of amylogenin cleavage
-
additional information
inhibitor design, determination of the features of the individual binding pockets of the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0195 - 0.585
amelogenin
-
0.0164
Mca-PLGL-Dpa-AR
37°C
0.0164
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2
at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031 - 0.77
amelogenin
-
8.1
Mca-PLGL-Dpa-AR
37°C
8.1
Mca-PLGL-[3-DNP-2,3-DAP]-AR-NH2
at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 1.9
amelogenin
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
presence of MMP20 at mRNA and protein level. MMP20 is coexpressed with dentin sialophosphoprotein DSPP. The MMP20-DSPP interaction is very intense and specific, and precludes MMP20 from interacting with the other members of the small integrin-binding ligand N-linked glycoproteins
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MMP20 is secreted
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
genetic defects in MMP20 are involved in the hypomaturation-type enamel defect
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP20_HUMAN
483
0
54387
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
57000
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure analysis and modeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
enzyme proform contains a prodomain motif PRCGVPD, the proform is in a latent state
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
solution structure of the catalytic domain of MMP-20 complexed with N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E227A
E235A
-
enzymatically inactive MMP-20
E352K
mutation identified in a family with hypomaturation-type enamel defect. Mutant protein is expressed at a normal level but secreted only minimally with proteolytic function. The homozygous change of glutamic acid to basic lysine in the hemopexin domain is predicted to result in a conformational change in MMP20
H226Q
T130I
mutant protein has reduced activity of MMP20
W34X
the nonsense mutation results in no functional MMP20 during tooth formation
Y180*/T130I
mutation identified in patients with hypomaturation amelogenesis imperfecta. Affected persons exhibit slight yellowish discoloration with reduced transparency
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel resin chromatography
purified on Ni column
-
recombinant from Escherichia coli
recombinant wild-type and inactive mutant E227A
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosome mapping to 11q22, expression in Escherichia coli BL21(DE3)
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expression in Escherichia coli
expression in Escherichia coli as an N-terminal His6 fusion
-
MMP20 DNA and amino acid sequenced determination and analysis, genotyping
MMP20 gene, DNA and amino acid sequence determination and analysis, allele-specific expression method, genotyping
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from inclusion bodies expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
enzyme is a potential target for selective inhibition and inhibitor design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Llano, E.; Pendas, A.M.; Knauper, V.; Sorsa, T.; Salo, T.; Salido, E.; Murphy, G.; Simmer, J.P.; Bartlett, J.D.; Lopez-Otin, C.
Identification and structural and functional characterization of human enamelysin (MMP-20)
Biochemistry
36
15101-15108
1997
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Stracke, J.O.; Fosang, A.J.; Last, K.; Mercuri, F.A.; Pendas, A.M.; Llano, E.; Perris, R.; Di Cesare, P.E.; Murphy, G.; Knauper, V.
Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)
FEBS Lett.
478
52-56
2000
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Ferreras, M.; Felbor, U.; Lenhard, T.; Olsen, B.R.; Delaisse, J.M.
Generation and degradation of human endostatin proteins by various proteinases
FEBS Lett.
486
247-251
2000
Homo sapiens
Manually annotated by BRENDA team
Terp, G.E.; Cruciani, G.; Christensen, I.T.; Jorgensen, F.S.
Structural differences of matrix metalloproteinases with potential implications for inhibitor selectivity examined by the GRID/CPCA approach
J. Med. Chem.
45
2675-2684
2002
Homo sapiens (O60882)
Manually annotated by BRENDA team
Turk, B.E.; Lee, D.H.; Yamakoshi, Y.; Klingenhoff, A.; Reichenberger, E.; Wright, J.T.; Simmer, J.P.; Komisarof, J.A.; Cantley, L.C.; Bartlett, J.D.
MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen
Biochemistry
45
3863-3874
2006
Homo sapiens, Mus musculus (Q3LRH7), Mus musculus
Manually annotated by BRENDA team
Kim, J.; Simmer, J.P.; Hart, T.C.; Hart, P.S.; Ramaswami, M.D.; Bartlett, J.D.; Hu, J.C.
MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta
J. Med. Genet.
42
271-275
2005
Homo sapiens
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
Zhang, Y.; Yan, Q.; Li, W.; DenBesten, P.K.
Fluoride down-regulates the expression of matrix metalloproteinase-20 in human fetal tooth ameloblast-lineage cells in vitro
Eur. J. Oral Sci.
114
105-110
2006
Homo sapiens
Manually annotated by BRENDA team
Arendt, Y.; Banci, L.; Bertini, I.; Cantini, F.; Cozzi, R.; Del Conte, R.; Gonnelli, L.
Catalytic domain of MMP20 (enamelysin) - The NMR structure of a new matrix metalloproteinase
FEBS Lett.
581
4723-4726
2007
Homo sapiens, Homo sapiens (O60882)
Manually annotated by BRENDA team
Tanimoto, K.; Le, T.; Zhu, L.; Witkowska, H.E.; Robinson, S.; Hall, S.; Hwang, P.; DenBesten, P.; Li, W.
Reduced amelogenin-MMP20 interactions in Amelogenesis imperfecta
J. Dent. Res.
87
451-455
2008
Homo sapiens, Homo sapiens (O60882)
Manually annotated by BRENDA team
Lu, Y.; Papagerakis, P.; Yamakoshi, Y.; Hu, J.C.; Bartlett, J.D.; Simmer, J.P.
Functions of KLK4 and MMP-20 in dental enamel formation
Biol. Chem.
389
695-700
2008
Homo sapiens (O60882)
Manually annotated by BRENDA team
Lee, S.K.; Seymen, F.; Kang, H.Y.; Lee, K.E.; Gencay, K.; Tuna, B.; Kim, J.W.
MMP20 hemopexin domain mutation in amelogenesis imperfecta
J. Dent. Res.
89
46-50
2010
Homo sapiens (O60882)
Manually annotated by BRENDA team
Wheeler, H.E.; Metter, E.J.; Tanaka, T.; Absher, D.; Higgins, J.; Zahn, J.M.; Wilhelmy, J.; Davis, R.W.; Singleton, A.; Myers, R.M.; Ferrucci, L.; Kim, S.K.
Sequential use of transcriptional profiling, expression quantitative trait mapping, and gene association implicates MMP20 in human kidney aging
PLoS Genet.
5
e1000685
2009
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Uskokovic, V.; Khan, F.; Liu, H.; Witkowska, H.E.; Zhu, L.; Li, W.; Habelitz, S.
Hydrolysis of amelogenin by matrix metalloprotease-20 accelerates mineralization in vitro
Arch. Oral Biol.
56
1548-1559
2011
Homo sapiens
Manually annotated by BRENDA team
Khan, F.; Liu, H.; Reyes, A.; Witkowska, H.E.; Martinez-Avila, O.; Zhu, L.; Li, W.; Habelitz, S.
The proteolytic processing of amelogenin by enamel matrix metalloproteinase (MMP-20) is controlled by mineral ions
Biochim. Biophys. Acta
1830
2600-2607
2013
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Koli, K.; Saxena, G.; Ogbureke, K.U.
Expression of matrix metalloproteinase (MMP)-20 and potential interaction with dentin sialophosphoprotein (DSPP) in human major salivary glands
J. Histochem. Cytochem.
63
524-533
2015
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Gomes-Silva, W.; Prado-Ribeiro, A.C.; Brandao, T.B.; Morais-Faria, K.; de Castro Junior, G.; Mak, M.P.; Lopes, M.A.; Rocha, M.M.; Salo, T.; Tjaederhane, L.; de Goes, M.F.; Santos-Silva, A.R.
Postradiation matrix metalloproteinase-20 expression and its impact on dental micromorphology and radiation-related caries
Caries Res.
51
216-224
2017
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Kim, Y.; Kang, J.; Seymen, F.; Koruyucu, M.; Gencay, K.; Shin, T.; Hyun, H.; Lee, Z.; Hu, J.; Simmer, J.; Kim, J.
Analyses of MMP20 missense mutations in two families with hypomaturation amelogenesis imperfecta
Front. Physiol.
8
229
2017
Homo sapiens (O60882), Homo sapiens
Manually annotated by BRENDA team
Seymen, F.; Park, J.C.; Lee, K.E.; Lee, H.K.; Lee, D.S.; Koruyucu, M.; Gencay, K.; Bayram, M.; Tuna, E.B.; Lee, Z.H.; Kim, Y.J.; Kim, J.W.
Novel MMP20 and KLK4 mutations in amelogenesis imperfecta
J. Dent. Res.
94
1063-1069
2015
Homo sapiens (O60882)
Manually annotated by BRENDA team
Ogbureke, K.U.; Koli, K.; Saxena, G.
Matrix metalloproteinase 20 co-expression with dentin sialophosphoprotein in human and monkey kidneys
J. Histochem. Cytochem.
64
623-636
2016
Homo sapiens (O60882), Homo sapiens, Macaca fascicularis (A0A2K5TT27)
Manually annotated by BRENDA team