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Merck
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文件

D9904

Sigma-Aldrich

Nα,Nε-Diacetyl-Lys-D-Ala-D-Ala

carboxypeptidase substrate

别名:

(Ac)2-L-Lys-D-Ala-D-Ala

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About This Item

经验公式（希尔记法）:
C16H28N4O6
CAS号:
24570-39-6
分子量:
372.42
MDL號碼:
MFCD00037235
分類程式碼代碼:
12352204
PubChem物質ID:
24894333
NACRES:
NA.32

品質等級

200

化驗

≥98% (HPLC)

形狀

powder

成份

Peptide content, ≥85%

溶解度

water: 50 mg/mL, clear, colorless

儲存溫度

−20°C

SMILES 字串

OC([C@@H](C)NC([C@@H](C)NC([C@@H](NC(C)=O)CCCCNC(C)=O)=O)=O)=O

InChI

1S/C16H28N4O6/c1-9(14(23)19-10(2)16(25)26)18-15(24)13(20-12(4)22)7-5-6-8-17-11(3)21/h9-10,13H,5-8H2,1-4H3,(H,17,21)(H,18,24)(H,19,23)(H,20,22)(H,25,26)

InChI 密鑰

VIHGYLJIMMKSBR-UHFFFAOYSA-N

基底

Substrate for penicillin-sensitive D-alanine carboxypeptidase.

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 3

閃點（°F）

Not applicable

閃點（°C）

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)

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Cleidiane G Zampronio et al.
Analytical chemistry, 76(17), 5172-5179 (2004-09-18)
Electrospray ionization (ESI) is extensively used in the analysis of biological compounds; yet some fundamental properties of this technique are not completely understood. It is widely recognized that care should be exercised when noncovalent complexes are being studied by ESI
T R Herrin et al.
Journal of medicinal chemistry, 28(9), 1371-1375 (1985-09-01)
A series of ristocetin analogues with modifications (OH, C=O, C=NOH, NCOCH3) at the C-1' amino group was synthesized and found to possess antibacterial activity against gram-positive bacteria and to bind to Ac2-Lys-D-Ala-D-Ala, a model for the antibiotic's site of action.
Zhibo Yang et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 15(9), 2081-2090 (2009-01-22)
Charge matters! The charge state significantly influences the conformation and the binding energy between vancomycin antibiotic and bacterial cell-wall analogue peptides (see figure). Surface-induced dissociation (SID) studies provide a quantitative comparison between the stabilities of different charge states of the
M Leyh-Bouille et al.
The Biochemical journal, 235(1), 177-182 (1986-04-01)
The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these compounds exert on the transpeptidase activity of the enzyme and, in the case
M Nguyen-Distèche et al.
The Biochemical journal, 207(1), 109-115 (1982-10-01)
The membrane-bound, 26 000-Mr penicillin-binding protein of Streptomyces K15 has been isolated in the form of an effective, penicillin-sensitive D-alanyl-D-alanine-cleaving peptidase exhibiting high transpeptidase activity (greater than 95%) and very low carboxy-peptidase activity (less than 5%). The penicillin-binding protein/transpeptidase can
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