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Literature summary for 3.2.1.14 extracted from

  • Dennhart, N.; Weigang, L.M.; Fujiwara, M.; Fukamizo, T.; Skriver, K.; Letzel, T.
    26kDa endochitinase from barley seeds: real-time monitoring of the enzymatic reaction and substrate binding experiments using electrospray ionization mass spectrometry (2009), J. Biotechnol., 143, 274-283.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E67Q loss of the enzymatic activity in E67Q is caused by a point mutation of Glu67 but not due to partial unfolding of the mutated enzyme Hordeum vulgare

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
x * 26000, SDS-PAGE Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
-
Hordeum vulgare GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + GlcNAcbeta(1-4)GlcNAcbeta
-
?
GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
-
Hordeum vulgare 2 GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc major product, plus some (GlcNAc)2 and (GlcNAc)4 ?
additional information no substrate: (GlcNAc)4, (GlcNAc)3, and (GlcNAc)2 Hordeum vulgare ?
-
?

Subunits

Subunits Comment Organism
? x * 26000, SDS-PAGE Hordeum vulgare