Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli | Serratia marcescens |
Protein Variants | Comment | Organism |
---|---|---|
F396A | site-directed mutagenesis of the +2 subsite residue of isozyme ChiA, the mutant shows only modest reductions in processivity, and shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan | Serratia marcescens |
W167A | site-directed mutagenesis of the -3 subsite residue of isozyme ChiA, the mutant shows almost abolished progressivity, reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan | Serratia marcescens |
W167A/W275A | site-directed mutagenesis of the -3 and +1 subsites residues of isozyme ChiA, the mutant shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan | Serratia marcescens |
W275A | site-directed mutagenesis of the +1 subsite residue of isozyme ChiA, the mutant shows only modest reductions in processivity, and shows reduced efficiency toward chitin and an up to 20fold higher activity toward chitosan | Serratia marcescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
chitin + H2O | Serratia marcescens | - |
? | - |
? | |
chitin + H2O | Serratia marcescens BJL200 | - |
? | - |
? | |
chitosan + H2O | Serratia marcescens | - |
? | - |
? | |
chitosan + H2O | Serratia marcescens BJL200 | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Serratia marcescens | - |
isozyme ChiA | - |
Serratia marcescens BJL200 | - |
isozyme ChiA | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Serratia marcescens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
chitin + H2O | - |
Serratia marcescens | ? | - |
? | |
chitin + H2O | crystalline beta-chitin, molecular weight analysis of oligomer products, overview | Serratia marcescens | ? | - |
? | |
chitin + H2O | - |
Serratia marcescens BJL200 | ? | - |
? | |
chitin + H2O | crystalline beta-chitin, molecular weight analysis of oligomer products, overview | Serratia marcescens BJL200 | ? | - |
? | |
chitosan + H2O | - |
Serratia marcescens | ? | - |
? | |
chitosan + H2O | soluble chitin-derivative chitosan, molecular weight analysis of oligomer products, overview | Serratia marcescens | ? | - |
? | |
chitosan + H2O | - |
Serratia marcescens BJL200 | ? | - |
? | |
chitosan + H2O | soluble chitin-derivative chitosan, molecular weight analysis of oligomer products, overview | Serratia marcescens BJL200 | ? | - |
? | |
additional information | aromatic residues in the catalytic center of chitinase A affect processivity, enzyme activity, and biomass converting efficiency. Progressivity of isozymes is dependent on the substrate, the processive mechanism is essential for an efficient conversion of crystalline substrates but comes at a large cost in terms of intrinsic enzyme speed, overview | Serratia marcescens | ? | - |
? | |
additional information | aromatic residues in the catalytic center of chitinase A affect processivity, enzyme activity, and biomass converting efficiency. Progressivity of isozymes is dependent on the substrate, the processive mechanism is essential for an efficient conversion of crystalline substrates but comes at a large cost in terms of intrinsic enzyme speed, overview | Serratia marcescens BJL200 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ChiA | - |
Serratia marcescens |
chitinases A | - |
Serratia marcescens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Serratia marcescens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.3 | - |
assay at | Serratia marcescens |