N-Benzylglycine
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N-Benzylglycine

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N-Benzylglycine is used as a replacement for aromatic amino acid residues in polypeptide analogues. This is done in order to determine the agonist or antagonist pharmacological properties of the analogue with respect to that specific amino acid. N-Benzylglycine is also used as a starting material to synthesize diazoketones.

Category
Other Unnatural Amino Acids
Catalog number
BAT-007718
CAS number
17136-36-6
Molecular Formula
C9H11NO2
Molecular Weight
165.19
N-Benzylglycine
IUPAC Name
2-(benzylamino)acetic acid
Synonyms
2-(Benzylamino)acetic acid; N-benzyl glycine; N-(Phenylmethyl)glycine; Glycine, N-(phenylmethyl)-; 2-[benzylamino]acetic acid; benzylglycine
Appearance
White to off-white crystalline powder
Purity
≥ 98% (HPLC)
Density
1.161±0.06 g/cm3 (Predicted)
Melting Point
232 °C (dec.)
Boiling Point
308.9±25.0 °C (Predicted)
Storage
Store at 2-8 °C
InChI
InChI=1S/C9H11NO2/c11-9(12)7-10-6-8-4-2-1-3-5-8/h1-5,10H,6-7H2,(H,11,12)
InChI Key
KGSVNOLLROCJQM-UHFFFAOYSA-N
Canonical SMILES
C1=CC=C(C=C1)CNCC(=O)O
1. Characterization of the FAD-containing N-methyltryptophan oxidase from Escherichia coli
P Khanna, M Schuman Jorns Biochemistry. 2001 Feb 6;40(5):1441-50. doi: 10.1021/bi0024411.
N-Methyltryptophan oxidase (MTOX) is a flavoenzyme that catalyzes the oxidative demethylation of N-methyl-L-tryptophan and other N-methyl amino acids, including sarcosine, which is a poor substrate. The Escherichia coli gene encoding MTOX (solA) was isolated on the basis of its sequence homology with monomeric sarcosine oxidase, a sarcosine-inducible enzyme found in many bacteria. These studies show that MTOX is expressed as a constitutive enzyme in a wild-type E. coli K-12 strain, providing the first evidence that solA is a functional gene. MTOX expression is enhanced 3-fold by growth on minimal media but not induced by N-methyl-L-tryptophan, L-tryptophan, or 3-indoleacrylate. MTOX forms an anionic flavin semiquinone and a reversible, covalent flavin-sulfite complex (K(d) = 1.7 mM), properties characteristic of flavoprotein oxidases. Rates of formation (k(on) = 5.4 x 10(-3) M(-1) s(-1)) and dissociation (k(off) = 1.3 x 10(-5) s(-1)) of the MTOX-sulfite complex are orders of magnitude slower than observed with most other flavoprotein oxidases. The pK(a) for ionization of oxidized FAD at N(3)H in MTOX (8.36) is two pH units lower than that observed for free FAD. The MTOX active site was probed by characterization of various substrate analogues that act as competitive inhibitors with respect to N-methyl-L-tryptophan. Qualitatively similar perturbations of the MTOX visible absorption spectrum are observed for complexes formed with various aromatic carboxylates, including benzoate, 3-indole-(CH(2))(n)-CO(2)(-) and 2-indole-CO(2)(-). The most stable complex with 3-indole-(CH(2))(n)-CO(2)(-) is formed with 3-indolepropionate (K(d) = 0.79 mM), a derivative with the same side chain length as N-methyl-L-tryptophan. Benzoate binding is enhanced upon protonation of a group in the enzyme-benzoate complex (pK(EL) = 6.87) but blocked by ionization of a group in the free enzyme (pK(E) = 8.41), which is attributed to N(3)H of FAD. Difference spectra observed for the aromatic carboxylate complexes are virtually mirror images of those observed with sarcosine analogues (N,N'-dimethylglycine, N-benzylglycine). Charge-transfer complexes are formed with 3-indoleacrylate, pyrrole-2-carboxylate, and CH(3)XCH(2)CO(2)(-) (X = S, Se, Te).
2. Potent bradykinin antagonists containing N-benzylglycine or N-benzyl-l-alanine in position 8
O Dawidowska, A Prahl, W Kowalczyk, I Derdowska, B Lammek, T H Wierzba, W Juzwa, K Neubert, J Zabrocki, B Olejniczak J Pept Res. 2004 Jan;63(1):29-35. doi: 10.1046/j.1399-3011.2004.00101.x.
Two new analogues of a previously designed bradykinin (BK) antagonist, d-Arg-Arg-Pro-Hyp-Gly-Thi-Ser-d-Phe-Thi-Arg, substituted in position 8 by N-benzylglycine and N-benzyl-l-alanine were designed, synthesized and bioassayed. The results show an impressive enhancement of B2 antagonistic potencies of both peptides in comparison with the model. In two further analogues these modifications were combined with acylation of the N-terminus with 1-adamantanacarboxylic acid. Acylated analogues exhibited higher antagonistic potency in comparison with the parent compounds, however, the range of effect was not as high as in previously described cases. The activity of analogues was assessed by their ability to inhibit vasodepressor response to exogenous BK (rat blood pressure test). Our results may be of value in the design of more potent BK antagonists.
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