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
NACRES:
NA.26
PubChem Substance ID:
UNSPSC Code:
12352209
MDL number:
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)
SMILES string
NC(=O)CCC(NC(=O)OCc1ccccc1)C(=O)NCC(O)=O
InChI key
SOUXAAOTONMPRY-UHFFFAOYSA-N
form
powder
storage temp.
−20°C
Quality Level
Application
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。
Biochem/physiol Actions
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。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
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)
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
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
Noriko Miwa et al.
Journal of bioscience and bioengineering, 127(3), 281-287 (2018-10-03)
A screening system using enrichment culture has been established with the aim of obtaining a novel enzyme for protein modification that has not been previously reported. This enzyme catalyzes deamidation of the side-chain amide group of asparagine in proteins. Enrichment
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