Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 227,741,298 papers from all fields of science
Search
Sign In
Create Free Account
6-nitro-3-phenylacetamidobenzoic acid
Known as:
2-nitro-5-phenylacetaminobenzoic acid
, Benzoic acid, 2-nitro-5-((phenylacetyl)amino)-
, NIPAB
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
3 relations
Broader (3)
Aminobenzoates
Aminobenzoic Acids
Nitrobenzoates
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2007
Highly Cited
2007
Permeation of 6-nitro-3-phenylacetamide benzoic acid (NIPAB) and hydrolysis by penicillin acylase immobilized in emulsion liquid membranes.
I. Miesiąc
,
K. Schügerl
,
J. Szymanowski
Journal of chemical technology and biotechnology
2007
Corpus ID: 27365584
The effects of various commercial and model surfactants of different structure and hydrophilicity were studied on water-in-oil (w…
Expand
2002
2002
Substrate specificity of penicillin acylase from Streptomyces lavendulae.
Raquel Torres‐Guzmán
,
I. de la Mata
,
Jesús Torres-Bacete
,
M. Arroyo
,
M. Castillón
,
C. Acebal
Biochemical and Biophysical Research…
2002
Corpus ID: 23292981
The kinetic parameters of several substrates of penicillin acylase from Streptomyces lavendulae have been determined. The enzyme…
Expand
1999
1999
Site-directed Mutagenesis of the Active Center of Penicillin Acylase from E. coli ATCC 11105.
Minghua Dai
,
E. Wang
,
Yong Xie
,
Weihong Jiang
,
Guoping Zhao
Sheng wu hua xue yu sheng wu wu li xue bao Acta…
1999
Corpus ID: 7168685
Site-directed mutagenesis and chemical modification were performed at Ser290 of the penicillin G acylase from E. coli ATCC11105…
Expand
1998
1998
Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in E. coli yields several active forms
Z. Ignatova
,
S. Stoeva
,
+5 authors
V. Kasche
Biotechnology Letters
1998
Corpus ID: 22844631
Of four enzymatically active forms of Alcaligenes faecalis penicillin amidase (EC 3.5.1.11) observed in sonicated cells, two (PA5…
Expand
Highly Cited
1997
Highly Cited
1997
Kinetic study of penicillin acylase from Alcaligenes faecalis
V. Svedas
,
D. Guranda
,
L. V. van Langen
,
F. van Rantwijk
,
R. Sheldon
FEBS Letters
1997
Corpus ID: 45204734
1995
1995
Cloning of penicillin G acylase-encoding gene from Escherichia coli high-producing strain RE3
L. Sobotková
,
V. Štěpánek
,
K. Plháčková
,
P. Kyslík
Biotechnology Letters
1995
Corpus ID: 27189201
SummaryPga gene from the industrial strain of E. coli RE3 hyperproducing penicillin G acylase (PGA) was cloned using a simple and…
Expand
Highly Cited
1993
Highly Cited
1993
Improved penicillin amidase production using a genetically engineered mutant of Escherichia coli ATCC 11105
N. Robas
,
H. Zouheiry
,
G. Branlant
,
C. Branlant
Biotechnology and Bioengineering
1993
Corpus ID: 25922079
Penicillin G amidase (PGA) is a key enzyme for the industrial production of penicillin G derivatives used in therapeutics…
Expand
1990
1990
Multiple potassium and chloride channels in the human colon carcinoma cell line SW1116.
R. Etcheberrigaray
,
S. Yedgar
,
E. Rojas
,
H. Pollard
Membrane Biochemistry
1990
Corpus ID: 754177
SW1116 cells have a profound capacity for secreting mucin molecules bearing the Lewisa epitope. Mucin molecules with the same…
Expand
1987
1987
Radiation-induced polymerization for the immobilization of penicillin acylase
E. Boccù
,
M. Carenza
,
S. Lora
,
G. Palma
,
F. Veronese
Applied Biochemistry and Biotechnology
1987
Corpus ID: 1740698
The immobilization ofEscherichia coli penicillin acylase (EC 3.5.1.11) was investigated by radiation-induced polymerization of 2…
Expand
1986
1986
A method for screening penicillin G acylase-producing bacteria by means of 2-nitro-5-phenylacetaminobenzoic acid test paper.
Q. -. Zhang
,
L. F. Zhang
,
H. Han
,
Y. Zhang
Analytical Biochemistry
1986
Corpus ID: 28252662
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE