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(2S,3S)-2-amino-6-(benzyloxy)-3-hydroxyhexanoic acid is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

168695-89-4

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168695-89-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 168695-89-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,6,8,6,9 and 5 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 168695-89:
(8*1)+(7*6)+(6*8)+(5*6)+(4*9)+(3*5)+(2*8)+(1*9)=204
204 % 10 = 4
So 168695-89-4 is a valid CAS Registry Number.

168695-89-4Relevant academic research and scientific papers

Engineered L-serine hydroxymethyltransferase from streptococcus thermophilus for the synthesis of α,α-dialkyl-α-amino acids

Bujons, Jordi,Claps, Pere,Hernandez, Karel,Joglar, Jesffls,Zelen, Igor,Usn, Isabel,Petrillo, Giovanna,Wandtke, Claudia M.,Parella, Teodor

, p. 3013 - 3017 (2015)

α,α-Disubstituted a-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5′-phosphate (PLP)-dependent l -serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth; EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of α,α-dialkyl-α-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.

An asymmetric total synthesis of a potent immunosuppressant, mycestericins D and F, through an aldol reaction using L-threonine aldolase

Nishide, Kiyoharu,Shibata, Kayoko,Fujita, Tetsuro,Kajimoto, Tetsuya,Wong, Chi-Huey,Node, Manabu

, p. 1191 - 1201 (2007/10/03)

L-Threonine aldolase from Candida humicola catalyzed the aldol reaction of 4-benzyloxybutanal (1) with glycine to give β-hydroxy-α-amino acids (2e,t), whose erythro / threo ratio was controlled by using either kinetic or thermodynamic conditions. The erythro derivative (4e) was effectively converted to mycestericins D and F via a stereoselective hydroxymethylation of oxazoline derivative (6) as the key step.

Kinetic and thermodynamic control of L-threonine aldolase catalyzed reaction and its application to the synthesis of mycestericin D

Shibata, Kayoko,Shingu, Kazushi,Vassilev, Vassil P.,Nishide, Kiyoharu,Fujita, Tetsuro,Node, Manabu,Kajimoto, Tetsuya,Wong, Chi-Huey

, p. 2791 - 2794 (2007/10/03)

L-Threonine aldolase catalyzes the aldol condensation of γ-benzyloxybutanal and glycine with high erythro/threo selectivity under a kinetically controlled condition. The erythro product was used in the synthesis of mycestericin D, a potent immunosuppressant.

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