Studies on the chemical modification of the essential groups of N-Acetyl-beta-D-glucosaminidase from viscera of green crab (Scylla Serrata).
The chemical modification of N-acetyl-beta-D: -glucosaminidase (EC3.2.1.30) from viscera of green crab (Scylla serrata) has been first studied. The modification of indole groups of tryptophan of the enzyme by N-bromosuccinimide can lead to complete inactivation, accompanying the absorption decreasing at 275 nm and the fluorescence intensity quenching at 338 nm, indicating that tryptophan is essential residue to the enzyme. The modification of histidine residue, the carboxyl groups, and lysine residue inactivates the enzyme completely or incompletely. The results show that imidazole groups of histidine residue or sulfhydryl residues, the carboxyl groups of acidic amino acid, amino groups of lysine residue, and indole groups of tryptophan were essential for the catalytic activity of enzyme, while the results demonstrate that the disulfide bonds and the carbamidine groups of arginine residues are not essential to the enzyme's function.
Jin
Zhu-Xing
ZX
Key Laboratory of Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Science, Xiamen University, Xiamen 361005, People's Republic of China.
Zhang
Ji-Ping
JP
Yan
Ya-Wen
YW
Wang
Qin
Q
D000085:Acetates / Q000737:chemistry; D000118:Acetylglucosaminidase / Q000737:chemistry* / Q000378:metabolism; D000601:Amino Acids, Essential / Q000737:chemistry*; D000818:Animals; D003386:Brachyura / Q000201:enzymology*; D002244:Carbon / Q000737:chemistry; D000077482:Carbon Fiber; D020134:Catalytic Domain; D004229:Dithiothreitol / Q000737:chemistry; D019704:Protein Disulfide-Isomerases / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry*
D000085:Acetates; D000601:Amino Acids, Essential; D000077482:Carbon Fiber; C016274:bromoacetate; D002244:Carbon; D014364:Tryptophan; D000118:Acetylglucosaminidase; D019704:Protein Disulfide-Isomerases; D004229:Dithiothreitol