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Literature summary for 4.2.2.2 extracted from

  • Kikuchi, T.; Shibuya, H.; Aikawa, T.; Jones, J.T.
    Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus (2006), Mol. Plant Microbe Interact., 19, 280-287.
    View publication on PubMed
Search for more literature for 4.2.2.2

Cloned(Commentary)

Cloned (Comment) Organism
pectate lyase BxPEL1 Bursaphelenchus xylophilus
pectate lyase BxPEL2 Bursaphelenchus xylophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ BxPEL1 shows full dependency Bursaphelenchus xylophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bursaphelenchus xylophilus the enzyme plays an important role in plant-nematode interactions ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bursaphelenchus xylophilus Q33CQ4
-
-
Bursaphelenchus xylophilus Q33CQ4 pectate lyase precursor
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme plays an important role in plant-nematode interactions Bursaphelenchus xylophilus ?
-
 ?
polygalacturonic acid the recombinant enzyme shows highest activity on polygalacturonic acid and lower activity on more highly methylated pectin Bursaphelenchus xylophilus ?
-
 ?

Synonyms

Synonyms Comment Organism
BxPEL1
-
 Bursaphelenchus xylophilus
BxPEL2
-
 Bursaphelenchus xylophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
 BxPEL1 Bursaphelenchus xylophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 10 BxPEL1 Bursaphelenchus xylophilus