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Reconstruction of Cysteine Biosynthesis Using Engineered Cysteine-Free and Methionine-Free EnzymesTen of the proteinogenic amino acids can be generated abiotically while the remaining thirteen require biology for their synthesis. Paradoxically, the biosynthesis pathways observed in nature require enzymes that are made with the amino acids they produce. For example, Escherichia coli produces cysteine from serine via two enzymes that contain cysteine. Here, we substituted alternate amino acids for cysteine and also methionine, which is biosynthesized from cysteine, in serine acetyl transferase (CysE) and O-acetylserine sulfhydrylase (CysM). CysE function was rescued by cysteine-and-methionine-free enzymes and CysM function was rescued by cysteine-free enzymes. Structural modeling suggests that methionine stabilizes CysM and is present in the active site of CysM. Cysteine is not conserved among CysE and CysM protein orthologs, suggesting that cysteine is not functionally important for its own synthesis. Engineering biosynthetic enzymes that lack the amino acids being synthesized provides insights into the evolution of amino acid biosynthesis and pathways for bioengineering.
Document ID
20160011209
Acquisition Source
Ames Research Center
Document Type
Preprint (Draft being sent to journal)
Authors
Wang, Kendrick (Stanford Univ. Stanford, CA, United States)
Fujishima, Kosuke (University Affiliated Research Center (Calif. Univ. Santa Cruz) Moffett Field, CA, United States)
Abe, Nozomi (Keio Univ. Tokyo, Japan)
Nakahigashi, Kenji (Keio Univ. Tokyo, Japan)
Endy, Drew (Stanford Univ. Stanford, CA, United States)
Rothschild, Lynn J. (NASA Ames Research Center Moffett Field, CA United States)
Date Acquired
September 13, 2016
Publication Date
January 1, 2016
Publication Information
Publisher: npg - Nature Publishing Group
Subject Category
Exobiology
Report/Patent Number
ARC-E-DAA-TN31972
Distribution Limits
Public
Copyright
Public Use Permitted.
Keywords
proteinogenic amino acids
biosynthesis
evolution of amino acid biosynthesis

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