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N-(4-Nitrophenyl)-L-glutamine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

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

Size	Price	Stock	Quantity
100 g	$4980	In stock

Specification
Reference Reading

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.