Discovery of McbB, an enzyme catalyzing the β-carboline skeleton construction in the marinacarboline biosynthetic pathway

Qi Chen; Changtao Ji; Yongxiang Song; Hongbo Huang; Junying Ma; Xinpeng Tian; Jianhua Ju

doi:10.1002/anie.201303449

Discovery of McbB, an enzyme catalyzing the β-carboline skeleton construction in the marinacarboline biosynthetic pathway

Angew Chem Int Ed Engl. 2013 Sep 16;52(38):9980-4. doi: 10.1002/anie.201303449. Epub 2013 Aug 1.

Authors

Qi Chen¹, Changtao Ji, Yongxiang Song, Hongbo Huang, Junying Ma, Xinpeng Tian, Jianhua Ju

Affiliation

¹ CAS Key Laboratory of Marine Bio-resources Sustainable Utilization, Guangdong Key Laboratory of Marine Materia Medica, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, 164 West Xingang Road, Guangzhou 510301 (China); University of Chinese Academy of Sciences, 19 Yuquan Road, Beijing 110039 (China).

PMID: 23913777
DOI: 10.1002/anie.201303449

Abstract

Three genes, mcbABC, that drive the biosynthesis of marinacarbolines, have been elucidated through genome mining, gene inactivation, heterologous expression, feeding, and site-directed mutagenesis experiments. McbB is highlighted as a novel enzyme for the β-carboline core construction, which involves a Pictet-Spengler cyclization process and requiring E97 for biochemical activity.

Keywords: Pictet-Spengler reaction; biosynthesis; marinacarbolines; natural products; β-carbolines.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Biological Products
Biosynthetic Pathways
Carbolines / chemical synthesis*
Carbolines / chemistry
Catalysis
Molecular Structure
Stereoisomerism

Substances

Biological Products
Carbolines