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3.4.24.65: macrophage elastase

This is an abbreviated version!
For detailed information about macrophage elastase, go to the full flat file.

Word Map on EC 3.4.24.65

Reaction

Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at -Ala14-/-Leu- and -Tyr16-/-Leu- in the B chain of insulin =

Synonyms

HME, hMMP-12, human macrophage elastase, Human macrophage metalloelastase, human metalloelastase, Macrophage elastase, macrophage matrix metalloproteinase, macrophage metalloelastase, macrophage-specific metalloelastase, matrix metalloproteinase 12, Matrix metalloproteinase-12, ME, Metalloelastase, MME, MMP-12, MMP12, More, mouse macrophage metalloelastase, rHME

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.65 macrophage elastase

Engineering

Engineering on EC 3.4.24.65 - macrophage elastase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A164V
-
mutation inconsequential to elastolysis
A182G
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
D124Q
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased (kcat/Km) toward fEln-100 compared to wild-type
D124Q/A182G
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/I180S
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/M156E
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant retains wild-type activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
D124Q/M156E/A182G
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is highly decreased compared to wild-type, compared to triple mutant D124Q/M156E/F185Y and D124Q/M156E/T205K catalytic efficacy toward fEln-100 is highly decreased
D124Q/M156E/F185Y
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is not affected compared to wild-type, compared to triple mutant D124Q/M156E/I180S and D124Q/M156E/A182G catalytic efficacy toward fEln-100 is moderately decreased
D124Q/M156E/I180S
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is highly decreased compared to wild-type, compared to triple mutant D124Q/M156E/F185Y and D124Q/M156E/T205K catalytic efficacy toward fEln-100 is highly decreased
D124Q/M156E/T205K
-
mutant confers a significantly greater loss of catalytic efficiency in digesting fEln-100 than the parental double mutant D124Q/M156E, catalytic activity toward MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is not affected compared to wild-type, compared to triple mutant D124Q/M156E/I180S and D124Q/M156E/A182G catalytic efficacy toward fEln-100 is moderately decreased
D200E
-
mutation inconsequential to elastolysis
E219A
G166R
-
mutation inconsequential to elastolysis
I180S
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
I255V
-
mutation inconsequential to elastolysis
K148T
-
mutation inconsequential to elastolysis
M103F
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased catalytic efficacy (kcat/Km) toward fEln-100 compared to wild-type
M156E
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows strong decreased (kcat/Km) toward fEln-100 compared to wild-type
M156E/A182G
-
kcat (fEln-100) is twice that of wild-type, mutant retains wild-type activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
M156E/I180S
-
combination of two well-separated mutations further reduces activity toward both fEln-100 and elastin-fluorescein compared to the single mutations, mutant shows decreased activity towards MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2
N153Y
-
mutation inconsequential to elastolysis
R117S
-
mutant retains similar activity toward substrate MCA-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 (Km and kcat similar to wild-type, kcat/Km), mutant shows decreased (kcat/Km) toward fEln-100 compared to wild-type
S142E
-
mutation inconsequential to elastolysis
V144A
-
mutation inconsequential to elastolysis
V162S
-
mutation inconsequential to elastolysis
Y132A
-
mutation inconsequential to elastolysis
additional information