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Literature summary for 4.2.2.3 extracted from

  • Li, J.; Dong, S.; Song, J.; Li, C.; Chen, X.; Xie, B.; Zhang, Y.
    Purification and characterization of a bifunctional alginate lyase from Pseudoalteromonas sp. SM0524 (2011), Mar. Drugs, 9, 109-123.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis aly-SJ02 may be a good tool to produce dimers and trimers from alginate Pseudoalteromonas sp.

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ slightly inhibiting Pseudoalteromonas sp.
EDTA 1 mM, 48% of initial activity; 51.7% inhibition at 1 mM Pseudoalteromonas sp.
Sn2+ slightly inhibiting Pseudoalteromonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information KM-value for alpha-L-guluronosyl linkage in alginate, 1.086 mg/ml, for poly(alpha-L-guluronic acid), 2.751 mg/ml at pH 8.5, 50°C Pseudoalteromonas sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Pseudoalteromonas sp.
-
-
extracellular aly-SJ02 is secreted Pseudoalteromonas sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ activates Pseudoalteromonas sp.
Ba2+ 1mM, 143% of initial activity Pseudoalteromonas sp.
Ca2+ activates Pseudoalteromonas sp.
Ca2+ 1mM, 136% of initial activity Pseudoalteromonas sp.
Co2+ activates Pseudoalteromonas sp.
Co2+ 1mM, 123% of initial activity Pseudoalteromonas sp.
K+ activates Pseudoalteromonas sp.
K+ 1mM, 117% of initial activity Pseudoalteromonas sp.
Mg2+ activates Pseudoalteromonas sp.
Mg2+ 1mM, 126% of initial activity Pseudoalteromonas sp.
Mn2+ 1mM, 116% of initial activity Pseudoalteromonas sp.
additional information Zn2+ has no effect on aly-SJ02 activity Pseudoalteromonas sp.
Na+ activates Pseudoalteromonas sp.
Na+ 1mM, 143% of initial activity Pseudoalteromonas sp.
NaCl aly-SJ02 shows the highest activity in 0.2 M NaCl, and retains more than 75% activity in 1 M NaCl, exhibiting salt-tolerance ability Pseudoalteromonas sp.
Ni2+ activates Pseudoalteromonas sp.
Ni2+ 1mM, 110% of initial activity Pseudoalteromonas sp.
Sr2+ activates Pseudoalteromonas sp.
Sr2+ 1mM, 124% of initial activity Pseudoalteromonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, SDS-PAGE Pseudoalteromonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudoalteromonas sp. alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG ?
-
?

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas sp.
-
bifunctional enzyme, actitivies against poly(beta-D-mannuronate), EC 4.2.2.3, and poly(alpha-L-guluronate), EC 4.2.2.11
-
Pseudoalteromonas sp.
-
from marine rotten kelp from a kelp culture field at the seashore of Yantai, China
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudoalteromonas sp.
native, secreted aly-SJ02 73.4fold by ultrafiltration, anion exchange chromatography, and gel filtration Pseudoalteromonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4803
-
pH 8.5, 50°C Pseudoalteromonas sp.
4803
-
purified enzyme, pH 8.5, 50°C Pseudoalteromonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-mannuronyl linkage in alginate
-
Pseudoalteromonas sp. ? enzyme shows activities toward both polyG, i.e.alpha-L-guluronic acid, and polyM, i.e. beta-D-mannuronic acid ?
additional information alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG Pseudoalteromonas sp. ?
-
?
poly(beta-(1->4)-D-mannuronate)
-
Pseudoalteromonas sp. ?
-
?

Subunits

Subunits Comment Organism
? x * 32000, SDS-PAGE Pseudoalteromonas sp.

Synonyms

Synonyms Comment Organism
alginate lyase
-
Pseudoalteromonas sp.
Aly-SJ02
-
Pseudoalteromonas sp.
polymannuronate lyase
-
Pseudoalteromonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Pseudoalteromonas sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3 65 assay range Pseudoalteromonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
half-life 41 min Pseudoalteromonas sp.
40
-
half-life is 41 min Pseudoalteromonas sp.
50
-
half-life 20 min Pseudoalteromonas sp.
50
-
half-life is 20 min Pseudoalteromonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Pseudoalteromonas sp.

pH Range

pH Minimum pH Maximum Comment Organism
5 10 assay range Pseudoalteromonas sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 11 at 25 °C for 20 min, the purified enzyme retains more than 50% activity at pH 7.0-10, aly-SJ02 is most stable at pH 8.0 Pseudoalteromonas sp.
8
-
most stable at pH 8.0 Pseudoalteromonas sp.

General Information

General Information Comment Organism
evolution N-terminal sequence analysis suggest that aly-SJ02 may be an alginate lyase of polysaccharide lyase family 18 Pseudoalteromonas sp.