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经验公式(希尔记法):
C15H12N2O5
化学文摘社编号:
分子量:
300.27
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
12352204
MDL number:
InChI
1S/C15H12N2O5/c18-14(8-10-4-2-1-3-5-10)16-11-6-7-13(17(21)22)12(9-11)15(19)20/h1-7,9H,8H2,(H,16,18)(H,19,20)
SMILES string
OC(=O)c1cc(NC(=O)Cc2ccccc2)ccc1[N+]([O-])=O
InChI key
QHVQEQRGDKOHHC-UHFFFAOYSA-N
assay
≥98%
form
powder
solubility
ethanol: 9.80-10.20 mg/mL, clear, faintly yellow to yellow
storage temp.
2-8°C
Quality Level
General description
6-Nitro-3-(phenylacetamido)benzoic acid is a chromogenic analog of penicillin.
Substrate for penicillin amidase.
signalword
Danger
hcodes
Hazard Classifications
Eye Dam. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
Q J Zhang et al.
Analytical biochemistry, 156(2), 413-416 (1986-08-01)
A simple, rapid assay for screening penicillin G acylase-producing bacteria is presented. The method is based on the formation of yellow 2-nitro-5-aminobenzoic acid by penicillin G acylase acting on 2-nitro-5-phenylacetaminobenzoic acid (NIPAB). NIPAB test paper is briefly applied to bacterial
Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11 105.
C Kutzbach et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 355(1), 45-53 (1974-01-01)
Direct spectrophotometric measurement of enzyme activity in heterogeneous systems with insoluble substrate or immobilized enzyme.
B Galunsky et al.
Analytical biochemistry, 221(1), 213-214 (1994-08-15)
Davide A Cecchini et al.
BMC biotechnology, 7, 54-54 (2007-09-12)
Immobilized Penicillin G Acylase (PGA) derivatives are biocatalysts that are industrially used for the hydrolysis of Penicillin G by fermentation and for the kinetically controlled synthesis of semi-synthetic beta-lactam antibiotics. One of the most used supports for immobilization is glyoxyl-activated
Wynand B L Alkema et al.
European journal of biochemistry, 269(8), 2093-2100 (2002-05-03)
Penicillin acylase of Escherichia coli catalyses the hydrolysis and synthesis of beta-lactam antibiotics. To study the role of hydrophobic residues in these reactions, we have mutated three active-site phenylalanines. Mutation of alphaF146, betaF24 and betaF57 to Tyr, Trp, Ala or
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