Unknown

Dataset Information

0

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


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.

SUBMITTER: Lu W 

PROVIDER: S-EPMC8168799 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC213156 | biostudies-other
| S-EPMC7221717 | biostudies-literature
| S-EPMC1460979 | biostudies-other
| S-EPMC7705670 | biostudies-literature
| PRJEB24738 | ENA
| S-EPMC2748416 | biostudies-literature
| S-EPMC7231510 | biostudies-literature
| S-EPMC7247824 | biostudies-literature
| S-EPMC6143143 | biostudies-literature
| S-EPMC8102479 | biostudies-literature