Literature summary extracted from
Ertesvag, H.; Erlien, F.; Skjak-Braek, G.; Rehm, B.H.A.; Valla, S.
Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase (1998), J. Bacteriol., 180, 3779-3784.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.2.3 |
expression in Escherichia coli |
Azotobacter vinelandii |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.2.2.3 |
Zn2+ |
1 mM ZnCl2 reduces the activity to 7.6% of the control level without Zn2+ added, 0.1 mM Zn2+ reduces the activity to 61% |
Azotobacter vinelandii |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
4.2.2.3 |
0.46 |
- |
alginate |
- |
Azotobacter vinelandii |
|
4.2.2.3 |
0.46 |
- |
alginate |
alginate rich in mannuronic acid |
Azotobacter vinelandii |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.2.2.3 |
NaCl |
activity is optimal at 0.35 M |
Azotobacter vinelandii |
|
4.2.2.3 |
Zn2+ |
1 mM ZnCl2, 92% loss of activity |
Azotobacter vinelandii |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.2.2.3 |
39000 |
- |
x * 39000, SDS-PAGE |
Azotobacter vinelandii |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.3 |
Azotobacter vinelandii |
- |
- |
- |
4.2.2.3 |
Azotobacter vinelandii |
O52195 |
alginate lyase precursor; recombinant |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
4.2.2.3 |
proteolytic modification |
signal peptide is cleaved off, leaving a mature protein of 39000 Da |
Azotobacter vinelandii |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.2.3 |
partial |
Azotobacter vinelandii |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.2.3 |
alginate |
alginate rich in mannuronic acids, the enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid bonds and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-beta-D-mannuronic acid bonds and alpha-L-guluronic acid-alpha-L-guluronic acid-bonds |
Azotobacter vinelandii |
oligouronides |
- |
? |
|
4.2.2.3 |
alginate |
enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-alpha-L-guluronic acid or alpha-L-guluronic acid-beta-D-mannuronic acid bonds |
Azotobacter vinelandii |
unsaturated algino-oligosaccharides |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.2.3 |
? |
x * 39000, SDS-PAGE |
Azotobacter vinelandii |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.2.2.3 |
8.1 |
8.4 |
- |
Azotobacter vinelandii |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
4.2.2.3 |
6.7 |
8.4 |
pH 6.7: about 50% of maximal activity, pH 8.1-8.4: optimum |
Azotobacter vinelandii |
pI Value
EC Number |
Organism |
Comment |
pI Value Maximum |
pI Value |
---|
4.2.2.3 |
Azotobacter vinelandii |
isoelectric focusing |
- |
5.1 |