C6154
Z-Gln-Gly
γ-glutamyl donor substrate
别名:
N2-[(phenylmethoxy)carbonyl]-L-glutaminyl-glycine
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关于此项目
经验公式（希尔记法）:
C15H19N3O6
化学文摘社编号:
分子量:
337.33
MDL编号:
UNSPSC代码:
12352209
PubChem化学物质编号:
NACRES:
NA.26
表单
powder
储存温度
−20°C
SMILES字符串
NC(=O)CCC(NC(=O)OCc1ccccc1)C(=O)NCC(O)=O
InChI
1S/C15H19N3O6/c16-12(19)7-6-11(14(22)17-8-13(20)21)18-15(23)24-9-10-4-2-1-3-5-10/h1-5,11H,6-9H2,(H2,16,19)(H,17,22)(H,18,23)(H,20,21)
InChI key
SOUXAAOTONMPRY-UHFFFAOYSA-N
相关类别
Amino Acid Sequence
Z-Gln-Gly
应用
用于分光光度法测定转谷氨酰胺酶(TGase)活性的γ--谷氨酰胺供体底物。 Z-Gln-Gly用于酶促合成N-连接的拟糖蛋白。
生化/生理作用
N-苄氧基羰基-L-谷氨酰胺甘氨酸（Z-Gln-Gly，Z-QG）可用作底物来区分和表征转谷氨酰胺酶（TGase），该酶催化含Gln和Lys的肽的翻译后共价交联。Z-QG通过表面修饰支持谷氨酰基水平的交联应用。
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
Natalie M Rachel et al.
Protein science : a publication of the Protein Society, 26(11), 2268-2279 (2017-09-01)
Microbial transglutaminase (MTG) is a practical tool to enzymatically form isopeptide bonds between peptide or protein substrates. This natural approach to crosslinking the side-chains of reactive glutamine and lysine residues is solidly rooted in food and textile processing. More recently
Evan A Wells et al.
Archives of biochemistry and biophysics, 643, 57-61 (2018-02-27)
The Ca2+-dependent deamidation and transamidation activities of transglutaminase 2 (TG2) are important to numerous physiological and pathological processes. Herein, we have examined the steady-state kinetics and 15(V/K) kinetic isotope effects (KIEs) for the TG2-catalyzed deamidation and transamidation of N-Benzyloxycarbonyl-l-Glutaminylglycine (Z-Gln-Gly)
Noriho Kamiya et al.
Methods in molecular biology (Clifton, N.J.), 751, 81-94 (2011-06-16)
Transglutaminase (TGase) is an enzyme that catalyzes the post-translational covalent cross-linking of Gln- and Lys-containing peptides and/or proteins according to its substrate specificity. We have recently designed a variety of Gln-donor fluorescent substrates of microbial transglutaminase (MTG) from Streptomyces mobaraensis
Gabe Javitt et al.
BMC biotechnology, 17(1), 23-23 (2017-03-02)
Microbial transglutaminase (mTG) is a robust enzyme catalyzing the formation of an isopeptide bond between glutamine and lysine residues. It has found use in food applications, pharmaceuticals, textiles, and biomedicine. Overexpression of soluble and active mTG in E. coli has
Syeda Warisul Fatima et al.
Bioresource technology, 287, 121391-121391 (2019-05-12)
This work studied the production of Transglutaminase (TGase) using wheat bran as carbon source. The medium components and culture conditions were optimized by statistical Box-Behnken response surface methodology. The release of active Transglutaminase was enhanced by adding (i) protease to
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