EC Number |
Protein Variants |
Reference |
---|
3.2.1.14 | 2S |
two spacer sequences in tandem, dramatic reduction relative to wild-type |
657013 |
3.2.1.14 | A283S |
Km-value for mutant enzyme for 4-methylumbelliferyl-N,N',N''-triacetylchitotriose is 0.8 mM versus 1 mM for wild-type enzyme and turnover number is 2.3 per sec versus 1.3 for wild-type enzyme. Inhibition by allosamidin, acetazolamide, and 8-chlorotheophylline are not significantly affected by the mutation, inhibition by kinetin is not detectable |
679172 |
3.2.1.14 | A442G |
isolation and analysis of the naturally occurring polymorphism of isozyme CHIT1 from Caucasian children with bronchial asthma and adult control individuals, the mutation does not play a major role in development of asthma in children |
665239 |
3.2.1.14 | ChiADELTA2 |
consits of chitin-binding domains ChBD2 and ChBD3 and catalytic domain B |
656022 |
3.2.1.14 | ChiADELTA3 |
consits of chitin-binding domain ChBD1 and catalytic domain A |
656022 |
3.2.1.14 | ChiADELTA4 |
consits only of catalytic domain B |
656022 |
3.2.1.14 | ChiADELTA5 |
consits only of catalytic domain A |
656022 |
3.2.1.14 | D125A |
nearly complete loss in activity |
655450 |
3.2.1.14 | D125N |
twofold lower turnover and twofold higher KM than wild-type, also active at higher pH-values |
655450 |
3.2.1.14 | D170A/E172Q |
improved binding afinities toward substrates (GlcNAc)5, (GlcNAc)6, and GlcNbeta-4(GlcNAc)4 |
708608 |