Examining the molecular characteristics of glycoside hydrolase family 20 β-N-acetylglucosaminidases with high activity

Figures & data

Figure 1. Partial amino acid sequence alignment of GH 20 GlcNAcases.

Table 1. Molecular characteristics of GH 20 GlcNAcases.

		P1			P2
GlcNAcase (PDB ID or accession no.)	Total coil/α-helix	Total amino acids	Amino acids building coils	Asp and Glu	Total amino acids	Amino acids building coils	Asp and Glu
Chb (1QBA)^[Citation17,Citation18]	1.48	43	19	5	56	17	8
HJ5Nag (ARJ33352)^[14]	1.49	42	36	7	11	3	3
JB10Nag (AQM74372)^[13]	1.96	24	20	3	55	27	6
Hex1 (3GH4)^[19]	1.24	24	20	2	11	4	2
HexA (2GJX)^[Citation20,Citation21]	1.04	21	6	1	31	9	6
SpHex (1M01)^[22]	1.22	24	20	2	11	3	1
OfHex1 (3NSM)^[Citation23,Citation24]	1.12	24	13	2	34	9	5

Figure 2. Structures of GH 20 GlcNAcases.

Tews I, Perrakis A, Oppenheim A, et al. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay–sachs disease. Nat Struct Mol Biol. 1996;3:638–648. PMID:8673609.

 Google Scholar

Tews I, Vincentelli R, Vorgias CE. N-Acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli. Gene. 1996;170:63–67. PMID:8621090.

 Google Scholar

Zhou JP, Song ZF, Zhang R, et al. Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance. BMC Biotechnol. 2017;17:37. PMID:28399848.

 Google Scholar

Zhou JP, Song ZF, Zhang R, et al. A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics. Extremophiles. 2017;21:699–709. PMID:28432475.

 Google Scholar

Sumida T, Ishii R, Yanagisawa T, et al. Molecular cloning and crystal structural analysis of a novel β-N-acetylhexosaminidase from Paenibacillus sp. TS12 capable of degrading glycosphingolipids. J Mol Biol. 2009;392:87–99. PMID:19524595.

 Google Scholar

Lemieux MJ, Mark BL, Cherney MM, et al. Crystallographic structure of human β-hexosaminidase A: interpretation of Tay–sachs mutations and loss of GM2 ganglioside hydrolysis. J Mol Biol. 2006;359:913–929. PMID:16698036.

 Google Scholar

Hou Y, Tse R, Mahuran DJ. Direct determination of the substrate specificity of the α-active site in heterodimeric β-hexosaminidase A. Biochemistry. 1996;35:3963–3969. PMID:8672428.

 Google Scholar

Mark BL, Wasney GA, Salo TJS, et al. Structural and functional characterization of Streptomyces plicatus β-N-acetylhexosaminidase by comparative molecular modeling and site-directed mutagenesis. J Biol Chem. 1998;273:19618–19624. PMID:9677388.

 Google Scholar

Liu TA, Zhang HT, Liu FY, et al. Structural determinants of an insect β-N-acetyl-D-hexosaminidase specialized as a chitinolytic enzyme. J Biol Chem. 2011;286:4049–4058. PMID:21106526.

 Google Scholar

Yang Q, Liu T, Liu FY, et al. A novel β-N-acetyl-D-hexosaminidase from the insect Ostrinia furnacalis (Guenee). FEBS J. 2008;275:5690–5702. PMID:18959754.

 Google Scholar