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Literature summary for 3.2.1.14 extracted from

  • Ubhayasekera, W.; Rawat, R.; Ho, S.W.; Wiweger, M.; Von Arnold, S.; Chye, M.L.; Mowbray, S.L.
    The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce (2009), Plant Mol. Biol., 71, 277-289.
    View publication on PubMed
Search for more literature for 3.2.1.14

Crystallization (Commentary)

Crystallization (Comment) Organism
bi-lobed structure with a wide cleft lined by conserved residues. Glu113 acts as the proton donor, and Glu122 as a general base Picea abies

Protein Variants

Protein Variants Comment Organism
Y158C inactive Picea abies

Organism

Organism UniProt Comment Textmining
Picea abies C0JR29 isoform ChiA4
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.015
-
 catalytic domain, pH 5.0, 37°C Picea abies
0.015
-
 native enzyme, pH 5.0, 37°C Picea abies

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
carboxymethylchitin-Remazol Brilliant Violet 5R + H2O
-
 Picea abies ?
-
 ?
chitin + H2O
-
 Picea abies GlcNAc + ?
-
 ?

General Information

General Information Comment Organism
physiological function class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, they are better suited for action on substrates where only small regions of chitin chain are accessibl. The intact enzyme shows antifungal acivtiy, while the catalytic subunit alone has very low antifungal activity Picea abies