Detail Information for IndEnz0009000083
IED ID IndEnz0009000083
Enzyme Type ID chitinase000083
Protein Name Chitinase
EC 3.2.1.14
Fragment
Gene Name
Organism Streptomyces violaceus (Streptomyces venezuelae)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces violaceus (Streptomyces venezuelae)
Enzyme Sequence EQPGGDKVNLGYFTN
Enzyme Length 15
Uniprot Accession Number P84754
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by divalent metal ions. Maximum inhibition observed with Ca(2+) while the least inhibition was observed with Fe(2+). Inhibited by high concentrations of GlcNAc. {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1};
DNA Binding
EC Number 3.2.1.14
Enzyme Function FUNCTION: Antifungal activity. Inhibits the mycelial growth of A.niger, A.alternata and H.sativum. {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. There is a 37.7% decrease in activity at pH 5 and a 39.8% decrease in activity at pH 9. {ECO:0000269|PubMed:16972135, ECO:0000269|Ref.1};
Pathway
nucleotide Binding
Features Chain (1); Non-terminal residue (1)
Keywords Antimicrobial;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Fungicide;Glycosidase;Hydrolase;Polysaccharide degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 1,639
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda