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Literature summary for 4.2.2.2 extracted from

  • Li, X.; Wang, H.; Zhou, C.; Ma, Y.; Li, J.; Song, J.
    Cloning, expression and characterization of a pectate lyase from Paenibacillus sp. 0602 in recombinant Escherichia coli (2014), BMC Biotechnol., 14, 18.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
environmental protection biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process Paenibacillus sp.
industry biotechnological applications of microbial pectate lyases in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process Paenibacillus sp.

Cloned(Commentary)

Cloned (Comment) Organism
gene pelN, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in recombinant Escherichia coli strain BL21(DE3) Paenibacillus sp.

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ causes a severe loss of activity, 88% inhibition at 0.5 mM, 97% at 1 mM Paenibacillus sp.
Ca2+ inhibitory above 1 mM Paenibacillus sp.
Cu2+ 20% inhibition at 0.5 mM Paenibacillus sp.
EDTA complete inhibition at 0.5 mM Paenibacillus sp.
Fe2+ 18% inhibition at 0.5 mM, 43% at 1 mM Paenibacillus sp.
Mn2+ 25% inhibition at 0.5 mM, 43% at 1 mM Paenibacillus sp.
additional information Triton X-100 and Tween-20 have a negligible influence on the activity at 0.5-1.0 mM Paenibacillus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, 7.3fold activation at 0.5 mM, 4.4fold at 1 mM, Ca2+-binding residues are D151, D173, and D177 in PelN Paenibacillus sp.
K+ 19% activation at 0.5 mM Paenibacillus sp.
Mg2+ 25% activation at 0.5 mM Paenibacillus sp.
Zn2+ 16% activation at 0.5 mM Paenibacillus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pectin Paenibacillus sp.
-
?
-
?
polygalacturonic acid Paenibacillus sp.
-
?
-
?

Organism

Organism UniProt Comment Textmining
Paenibacillus sp. W8CR80 gene pelN
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme PelN 3fold from Escherichia coli strain BL21(DE3) Paenibacillus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2060
-
purified recombinant enzyme, pH 9.8, 65°C Paenibacillus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PelN exhibits relatively high activity on methylated substrates. On pectin with relatively low degree (20-34%) of methylation, the remaining specific activity of PelN is approximately 100% of that on polygalacturonic acid. Highly methylated pectin (55-70%) results in slight inhibition of the PelN activity to 74% Paenibacillus sp. ?
-
?
pectin
-
Paenibacillus sp. ?
-
?
polygalacturonic acid
-
Paenibacillus sp. ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
Paenibacillus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 75 activity range, recombinant enzyme, 14.8% of maximal activity at 35°C, 18% at 75°C Paenibacillus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 50 purified recombinant PelN displays a half-life of around 9 h and 42 h at 50°C and 45°C, respectively Paenibacillus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.8
-
-
Paenibacillus sp.

pH Range

pH Minimum pH Maximum Comment Organism
7.6 10.4 activity range, recombinant enzyme Paenibacillus sp.

General Information

General Information Comment Organism
evolution the enzyme belongs to the polysaccharide lyase family 1 Paenibacillus sp.
additional information invariant amino acids involved in catalytic function mainly comprised the catalytic residues R275, K244, and R280, and the Ca2+-binding residues D151, D173, and D177 in PelN Paenibacillus sp.