Literature summary extracted from
Lee, S.; Park, H.I.; Sang, Q.X.
Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion (2007), Biochem. J., 403, 31-42.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.24.B7 |
expression in Escherichia coli. Human breast cancer cell line, MDA-MB-231, transfected with wild-type MMP-26 cDNA shows a calcium-dependent invasive potential when compared with controls that were transfected with an inactive form of MMP-26 (E209A) |
Homo sapiens |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.24.B7 |
D114A |
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis |
Homo sapiens |
3.4.24.B7 |
D114A |
mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively |
Homo sapiens |
3.4.24.B7 |
D165A |
very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26 |
Homo sapiens |
3.4.24.B7 |
E191A |
very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26 |
Homo sapiens |
3.4.24.B7 |
E209A |
inactive mutant enzyme |
Homo sapiens |
3.4.24.B7 |
K189E |
calcium-independent high invasiveness is observed in the K189E mutant MDA-MB-231 cell line |
Homo sapiens |
3.4.24.B7 |
K189E |
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis |
Homo sapiens |
3.4.24.B7 |
K189E |
mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively |
Homo sapiens |
3.4.24.B7 |
V184D |
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis |
Homo sapiens |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.4.24.B7 |
Ca2+ |
MMP-26 has one high-affinity and one low-affinity calcium binding site. High-affinity calcium binding is restored at physiologically low calcium conditions with a calcium-dissociation constant of 63 nM without inducing secondary and tertiary structural changes. Low-affinity calcium binding is restored at relatively high calcium concentrations and shows a low-affinity calcium-dissociation constant value of 0.12 mM, which is accompanied with the recovery of enzymatic activity reversibly and tertiary structural changes, but without secondary structural rearrangements |
Homo sapiens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.B7 |
Homo sapiens |
- |
- |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.24.B7 |
endometase/matrilysin-2 |
- |
Homo sapiens |
3.4.24.B7 |
MMP-26 |
- |
Homo sapiens |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
3.4.24.B7 |
additional information |
- |
high-affinity calcium binding protects MMP-26 against thermal denaturation |
Homo sapiens |