Kevin D. Walker

Affiliations: 
Cell and Molecular Biology Michigan State University, East Lansing, MI 
Area:
Molecular Biology, Organic Chemistry
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"Kevin Walker"
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Publications

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Sullivan SA, Nawarathne I, Walker KD. (2020) CoA recycling by a benzoate coenzyme a ligase in cascade reactions with aroyltransferases to biocatalyze paclitaxel analogs. Archives of Biochemistry and Biophysics. 108276
Shee PK, Ratnayake ND, Walter T, et al. (2019) Exploring the Scope of an α/β-Aminomutase for the Amination of Cinnamate Epoxides to Arylserines and Arylisoserines Acs Catalysis. 9: 7418-7430
Attanayake G, Walter T, Walker KD. (2018) Understanding Which Residues of the Active Site and Loop Structure of a Tyrosine Aminomutase Define its Mutase and Lyase Activities. Biochemistry
Thornburg CK, Walter T, Walker KD. (2017) Biocatalysis of a Paclitaxel Analogue: Conversion of Baccatin III to N-Debenzoyl-N-(2-furoyl)paclitaxel and Characterization of an Amino Phenylpropanoyl CoA Transferase. Biochemistry
Muchiri R, Walker KD. (2017) Paclitaxel Biosynthesis: Adenylation and Thiolation Domains of an NRPS TycA PheAT Module Produce Various Arylisoserine CoA Thioesters. Biochemistry
Sa N, Rawat R, Thornburg C, et al. (2016) Identification and characterization of the missing phosphatase on the riboflavin biosynthesis pathway in Arabidopsis thaliana. The Plant Journal : For Cell and Molecular Biology
Walter T, Wijewardena D, Walker KD. (2016) Mutation of Aryl Binding-Pocket Residues Results in an Unexpected Activity Switch in an Oryza sativa Tyrosine Aminomutase. Biochemistry
Walter T, King Z, Walker KD. (2015) A Tyrosine Aminomutase from Rice (Oryza sativa) Isomerizes (S)-α- to (R)-β-Tyrosine with Unique High Enantioselectivity and Retention of Configuration. Biochemistry
Ratnayake ND, Theisen C, Walter T, et al. (2015) Whole-Cell Biocatalytic Production of Variously Substituted β-Aryl- and β-Heteroaryl-β-Amino Acids. Journal of Biotechnology
Thornburg CK, Wortas-Strom S, Nosrati M, et al. (2015) Kinetically and Crystallographically Guided Mutations of a Benzoate CoA Ligase (BadA) Elucidate Mechanism and Expand Substrate Permissivity. Biochemistry. 54: 6230-42
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