3ozo

Structural highlights

Function

HEXC_OSTFU Hydrolyzes one beta-GlcNAc unit at a time from the non-reducing ends of substrates, with a preference for shorter substrates. The 2-acetamido group and the beta-glycoside bond linkage in the substrate are required for its activity. Active with p-nitrophenyl (pNP)-beta-GlcNAc, pNP-beta-GalNAc and chitooligosaccharides (degree of polymerization from 2 to 6), but not with the complex N-glycan substrate (GlcNAcbeta-1,2Manalpha-1,6)(GlcNAcbeta-1,2Manalpha-1,3)Manbeta-1,4GlcNAcbeta-1,4GlcNAc-PA (GnGn-PA), pNP-alpha-GlcNAc or with the long polymer colloidal chitin. Involved in chitin catabolism (PubMed:18959754). Involved in the degradation of old cuticle during the pupation stage (PubMed:21106526).^{[1] [2]}

See Also

• Beta-Hexosaminidase
• Beta-Hexosaminidase 3D structures
• Beta-N-acetylhexosaminidase 3D structures

References

1. ↑ Yang Q, Liu T, Liu F, Qu M, Qian X. A novel beta-N-acetyl-D-hexosaminidase from the insect Ostrinia furnacalis (Guenée). FEBS J. 2008 Nov;275(22):5690-702. PMID:18959754 doi:10.1111/j.1742-4658.2008.06695.x
2. ↑ Liu T, Zhang H, Liu F, Wu Q, Shen X, Yang Q. Structural Determinants of an Insect {beta}-N-Acetyl-D-hexosaminidase Specialized as a Chitinolytic Enzyme. J Biol Chem. 2011 Feb 11;286(6):4049-58. Epub 2010 Nov 24. PMID:21106526 doi:10.1074/jbc.M110.184796