N-(4-Nitrophenyl)-L-glutamine
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N-(4-Nitrophenyl)-L-glutamine

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N-(4-Nitrophenyl)-L-glutamine is a substrate for γ-glutamyltransferase (GGT), which is an important enzyme with wide applications in biocatalysis and clinical diagnosis.

Category
L-Amino Acids
Catalog number
BAT-002168
CAS number
7300-59-6
Molecular Formula
C11H13N3O5
Molecular Weight
267.238
N-(4-Nitrophenyl)-L-glutamine
Size Price Stock Quantity
100 g $4980 In stock
IUPAC Name
(2S)-2-amino-5-(4-nitroanilino)-5-oxopentanoic acid
Synonyms
(S)-2-Amino-5-((4-nitrophenyl)amino)-5-oxopentanoic acid; L-gamma-Glutamyl-p-nitroanilide; L-Glutamic acid γ-p-nitroanilide; H-Glu(pNA)-OH
Appearance
cream coloured to light yellow powder
Purity
≥ 98%
Density
1.5±0.1 g/cm3
Melting Point
185-188°C
Boiling Point
590.6±50.0 °C at 760 mmHg
Storage
Sotre at 2-8°C
InChI
InChI=1S/C11H13N3O5/c12-9(11(16)17)5-6-10(15)13-7-1-3-8(4-2-7)14(18)19/h1-4,9H,5-6,12H2,(H,13,15)(H,16,17)/t9-/m0/s1
InChI Key
WMZTYIRRBCGARG-VIFPVBQESA-N
Canonical SMILES
C1=CC(=CC=C1NC(=O)CCC(C(=O)O)N)[N+](=O)[O-]
1.Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296.
Wetterholm A1, Medina JF, R?dmark O, Shapiro R, Haeggstr?m JZ, Vallee BL, Samuelsson B. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9141-5.
The metal-binding motif in the sequence of leukotriene A4 (LTA4) (EC 3.3.2.6), a bifunctional zinc metalloenzyme, contains a glutamic acid that is conserved in several zinc hydrolases. To study its role for the two catalytic activities, Glu-296 in mouse leukotriene A4 hydrolase was replaced by a glutamine or alanine residue by site-directed mutagenesis. Wild-type and mutated cDNAs were expressed four or five times in Escherichia coli, and the resulting proteins were purified to apparent homogeneity. With respect to their epoxide hydrolase activities--i.e., the conversion of LTA4 into leukotriene B4--the mutated enzymes [Gln296]LTA4 hydrolase and [Ala296]LTA4 hydrolase exhibited specific activities of 1070 +/- 160 and 90 +/- 30 nmol of LTB4 per mg of protein per min (mean +/- SD; n = 4 or 5), respectively, corresponding to 150% and 15% of unmutated enzyme. In contrast, when the mutated proteins were assayed for peptidase activity toward alanine-4-nitroanilide, they were found to be virtually inactive (less than or equal to 0.
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