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About This Item
经验公式（希尔记法）:
C16H28N4O6
CAS号:
分子量:
372.42
MDL號碼:
分類程式碼代碼:
12352204
PubChem物質ID:
NACRES:
NA.32
推荐产品
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)
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.
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
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
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 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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