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Merck
모든 사진(1)

문서

C6154

Sigma-Aldrich

Z-Gln-Gly

γ-glutamyl donor substrate

동의어(들):

N2-[(phenylmethoxy)carbonyl]-L-glutaminyl-glycine

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About This Item

실험식(Hill 표기법):
C15H19N3O6
CAS Number:
Molecular Weight:
337.33
MDL number:
UNSPSC 코드:
12352209
PubChem Substance ID:
NACRES:
NA.26

형태

powder

저장 온도

−20°C

SMILES string

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

Amino Acid Sequence

Z-Gln-Gly

애플리케이션

γ-Glutamyl donor substrate used in spectrophotometric determination of transglutaminase (TGase) activity. Z-Gln-Gly was used to enzymatically synthesize N-linked neoglycoproteins.

생화학적/생리학적 작용

N-Benzyloxycarbonyl-L-Glutaminylglycine (Z-Gln-Gly, Z-QG) is used as a substrate to differentiate and characterize transglutaminase(s) (TGase) that catalyzes the post-translational covalent cross-linking of Gln- and Lys-containing peptides. Z-QG supports glutamyl-level cross-linking applications thruough surface modification.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리 방문

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
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
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)
Momoko Kitaoka et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 17(19), 5387-5392 (2011-04-07)
A new synthetic strategy for DNA-enzyme conjugates with a novel architecture was explored using a natural cross-linking catalyst, microbial transglutaminase (MTG). A glutamine-donor substrate peptide of MTG was introduced at the 5-position on the pyrimidine of deoxyuridine triphosphate to prepare

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