D9904
Nα,Nε-Diacetyl-Lys-D-Ala-D-Ala
carboxypeptidase substrate
别名:
(Ac)2-L-Lys-D-Ala-D-Ala
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关于此项目
经验公式（希尔记法）:
C16H28N4O6
化学文摘社编号:
分子量:
372.42
MDL编号:
UNSPSC代码:
12352204
PubChem化学物质编号:
NACRES:
NA.32
质量水平
方案
≥98% (HPLC)
表单
powder
组成
Peptide content, ≥85%
溶解性
water: 50 mg/mL, clear, colorless
储存温度
−20°C
SMILES字符串
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 key
VIHGYLJIMMKSBR-UHFFFAOYSA-N
一般描述
Substrate for penicillin-sensitive D-alanine carboxypeptidase.
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)
法规信息
常规特殊物品
此项目有
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
Dual nano-electrospray for probing solution interactions and fast reactions of complex biomolecules.
Lewis P Mark et al.
European journal of mass spectrometry (Chichester, England), 18(5), 439-446 (2012-12-12)
A novel nano-electrospray emitter has been developed containing two separated channels running throughout the length of the emitter. The emitters have been fabricated from "theta-shaped" borosilicate capillaries. Loading of different solutions into the two different channels opens up the possibility
Conformational analysis of peptide substrates and inhibitors of the Zn2+ G and serine R61 D-alanyl-D-alanine peptidases.
J L De Coen et al.
European journal of biochemistry, 121(1), 221-232 (1981-12-01)
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
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.
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