Levocarnitine Impurity 18

Name: Levocarnitine Impurity 18 | 84367-31-7
Brand: US-CATO
SKU: S57C4X-129218_20_MG
Price: 19998.0 USD
Availability: InStock

Cat. No S57C4X-129218_20_MG

Vendor: US-CATO

Product Information

Product Name

Levocarnitine Impurity 18

Brand Name

US-CATO

Product Number

C4X-129218

CAS

84367-31-7

Certificate of Analysis (COA)

COA not found

General Information

PubChem CID

641056

IUPAC Name

(3R)-4-chloro-3-hydroxybutanenitrile

InChI Key

LHBPNZDUNCZWFL-SCSAIBSYSA-N

SMILES

C(C#N)C@H(CCl)O

References Data Source From Pubchem

Biocatalytic approaches for the synthesis of optically pure vic-halohydrins

Publication Name: Applied Microbiology and Biotechnology

Publication Date: 2021-04-13

DOI: 10.1007/s00253-021-11266-2

Significant improvement of the enantioselectivity of a halohydrin dehalogenase for asymmetric epoxide ring opening reactions by protein engineering

Publication Name: Applied Microbiology and Biotechnology

Publication Date: 2020-01-14

DOI: 10.1007/s00253-020-10356-x

Recent advances on halohydrin dehalogenases—from enzyme identification to novel biocatalytic applications

Publication Name: Applied Microbiology and Biotechnology

Publication Date: 2016-08-08

DOI: 10.1007/s00253-016-7750-y

Cascade Reactions Using a Single Enzyme

Publication Name: Science of Synthesis

Publication Date: 2015

Production of Chiral C3- and C4-Units by Microbial Enzymes

Publication Name: Advances in Biochemical Engineering/Biotechnology

Publication Date: 1999

DOI: 10.1007/3-540-69791-8_5

Levocarnitine Impurity 18

Product Information

General Information

References Data Source From Pubchem

Biocatalytic approaches for the synthesis of optically pure vic-halohydrins

Significant improvement of the enantioselectivity of a halohydrin dehalogenase for asymmetric epoxide ring opening reactions by protein engineering

Recent advances on halohydrin dehalogenases—from enzyme identification to novel biocatalytic applications

Cascade Reactions Using a Single Enzyme

Production of Chiral C3- and C4-Units by Microbial Enzymes