Z-L-alanine
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Z-L-alanine

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Category
CBZ-Amino Acids
Catalog number
BAT-003319
CAS number
1142-20-7
Molecular Formula
C11H13NO4
Molecular Weight
223.20
Z-L-alanine
IUPAC Name
(2S)-2-(phenylmethoxycarbonylamino)propanoic acid
Synonyms
Z-L-Ala-OH; N-Benzyloxycarbonyl-L-Alanine
Appearance
White to off-white crystalline powder
Purity
≥ 99.5% (Chiral HPLC)
Density
1.2446 g/cm3(rough estimate)
Melting Point
80-90 °C
Boiling Point
364.51°C (rough estimate)
Storage
Store at 2-8°C
InChI
InChI=1S/C11H13NO4/c1-8(10(13)14)12-11(15)16-7-9-5-3-2-4-6-9/h2-6,8H,7H2,1H3,(H,12,15)(H,13,14)/t8-/m0/s1
InChI Key
TYRGLVWXHJRKMT-QMMMGPOBSA-N
Canonical SMILES
CC(C(=O)O)NC(=O)OCC1=CC=CC=C1

Z-L-alanine, an amino acid derivative with diverse applications in bioscience and industry, offers a myriad of possibilities. Here are the key applications characterized by high perplexity and burstiness:

Peptide Synthesis: Serving as a fundamental building block in peptide and protein synthesis, Z-L-alanine plays a pivotal role in unraveling the intricacies of protein structure and function. By integrating Z-L-alanine into peptide chains researchers embark on a journey to explore new dimensions in therapeutics and delve deeper into biochemical pathways illuminating the path towards groundbreaking discoveries.

Chiral Synthesis: Embodying unique stereochemical properties, Z-L-alanine emerges as a cornerstone in chiral synthesis acting as a linchpin in the creation of enantiomerically pure compounds. These chiral entities find their place of prominence in pharmaceuticals agrochemicals and fine chemicals sectors where stereochemistry reigns supreme in determining efficacy and safety standards shaping the landscape of modern industry.

Biocatalysis: Delving into the realm of biocatalysis, Z-L-alanine takes center stage in studying enzyme kinetics and specificity unveiling the mysteries of catalytic mechanisms and substrate interactions. Enzymes catalyzing Z-L-alanine offer invaluable insights into the intricate dance of biochemical reactions paving the way for the development of novel enzymes essential for industrial processes and therapeutic breakthroughs heralding a new era of innovation.

Nutritional Research: The multifaceted role of Z-L-alanine in nutritional and metabolic spheres beckons researchers to uncover its vast potential across various organisms. Investigating the metabolic and nutritional functions of Z-L-alanine sheds light on its role in protein metabolism and energy generation fostering the development of cutting-edge nutritional supplements and the optimization of animal feed formulations pushing the boundaries of nutritional science.

1. Studies on the biodegradation of fosfomycin: synthesis of 13C-labeled intermediates, feeding experiments with Rhizobium huakuii PMY1, and isolation of labeled amino acids from cell mass by HPLC
John W McGrath, Friedrich Hammerschmidt, Hanspeter Kählig, Frank Wuggenig, Günther Lamprecht, John P Quinn Chemistry. 2011 Nov 18;17(47):13341-8. doi: 10.1002/chem.201100725. Epub 2011 Oct 20.
Racemic (1R*,2R*)-1,2-dihydroxy-[1-(13)C(1)]propylphosphonic acid and 1-hydroxy-[1-(13)C(1)]acetone were synthesized and fed to R. huakuii PMY1. Alanine and a mixture of valine and methionine were isolated as their N-acetyl derivatives from the cell hydrolysate by reversed-phase HPLC and analyzed by NMR spectroscopy. It was found that the carbon atoms of the respective carboxyl groups were highly (13)C-labeled (up to 65 %). Hydroxyacetone is therefore considered an obligatory intermediate of the biodegradation of fosfomycin by R. huakuii PMY1.
2. On the transformation of (S)-2-hydroxypropylphosphonic acid into fosfomycin in Streptomyces fradiae--a unique method of epoxide ring formation
Anna Woschek, Frank Wuggenig, Wolfgang Peti, Friedrich Hammerschmidt Chembiochem. 2002 Sep 2;3(9):829-35. doi: 10.1002/1439-7633(20020902)3:93.0.CO;2-V.
(1S,2S)- and (1R,2S)-2-hydroxy-[1-D(1)]propylphosphonic acid were synthesised from (1S,2S)-2-benzyloxy-[1-D(1)]propanol, which was obtained by horse liver alcohol dehydrogenase catalysed reduction of the corresponding aldehyde. When (1S,2S)-2-hydroxy-[1-D(1)]propylphosphonic acid was fed to Streptomyces fradiae, the deuterium was retained to the same extent in fosfomycin (cis-epoxide) and its co-metabolite trans-epoxide. Removal of the hydrogen (deuterium) atom from the C-1 atom of deuterated 2-hydroxypropylphosphonic acids is a stereospecific process (the hydrogen atom of (S)-2-hydroxypropylphosphonic acid is pro-R). The formation of the O--C-1 bond of fosfomycin occurs with net inversion of configuration, the formation of the O--C-1 bond of the trans-epoxide with net retention.
3. Studies on the biodegradation of fosfomycin: growth of Rhizobium huakuii PMY1 on possible intermediates synthesised chemically
John W McGrath, Friedrich Hammerschmidt, Werner Preusser, John P Quinn, Anna Schweifer Org Biomol Chem. 2009 May 7;7(9):1944-53. doi: 10.1039/b821829c. Epub 2009 Mar 23.
The first step of the mineralisation of fosfomycin by R. huakuii PMY1 is hydrolytic ring opening with the formation of (1R,2R)-1,2-dihydroxypropylphosphonic acid. This phosphonic acid and its three stereoisomers were synthesised by chemical means and tested as their ammonium salts for mineralisation as evidenced by release of P(i). Only the (1R,2R)-isomer was degraded. A number of salts of phosphonic acids such as (+/-)-1,2-epoxybutyl-, (+/-)-1,2-dihydroxyethyl-, 2-oxopropyl-, (S)-2-hydroxypropyl-, (+/-)-1-hydroxypropyl- and (+/-)-1-hydroxy-2-oxopropylphosphonic acid were synthesised chemically, but none supported growth. In vitro C-P bond cleavage activity was however detected with the last phosphonic acid. A mechanism involving phosphite had to be discarded as it could not be used as a phosphorus source. R. huakuii PMY1 grew well on (R)- and (S)-lactic acid and hydroxyacetone, but less well on propionic acid and not on acetone or (R)- and (+/-)-1,2-propanediol. The P(i) released from (1R,2R)-1,2-dihydroxypropylphosphonic acid labelled with one oxygen-18 in the PO3H2 group did not stay long enough in the cells to allow complete exchange of 18O for 16O by enzymic turnover.
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