MarH, a Bifunctional Enzyme Involved in the Condensation and Hydroxylation Steps of the Marineosin Biosynthetic Pathway

Authors

Wanli Lu, Portland State Univesity
Papireddy Kancharla, Portland State UnivesityFollow
Kevin A. Reynolds, Portland State UnivesityFollow

Published In

Organic Letters

Document Type

Citation

Publication Date

3-1-2017

Abstract

A novel bifunctional enzyme, MarH, has been identified, and its key functional role in the marineosin biosynthesis successfully probed. MarH catalyzes (1) a condensation step between 4-methoxy-2,2′-bipyrrole-5-carboxaldehyde (MBC) and 2-undecylpyrrole (UP) to form undecylprodiginine (UPG) and (2) hydroxylation of the alkyl chain of UPG to form the (S)-23-hydroxyundecylprodiginine (HUPG), which is essential for MarG catalyzed bicyclization toward the formation of an unusual spiro-tetrahydropyran-aminal ring of marineosins. The final enigmatic steps in the marineosin biosynthesis have now been deciphered.

Locate the Document

https://doi.org/10.1021/acs.orglett.7b00093

DOI

10.1021/acs.orglett.7b00093

Persistent Identifier

https://archives.pdx.edu/ds/psu/27027

Citation Details

Lu W., Kancharla P., Reynolds K.A. 2017. MarH, a Bifunctional Enzyme Involved in the Condensation and Hydroxylation Steps of the Marineosin Biosynthetic Pathway, Organic Letters, 19(6):1298-1301.