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A four-protein metabolon assembled by a small peptide protein creates the pentacyclic carbonate ring of aldgamycins

Authors :
Guo-Dong Chen
Dan Hu
Xiao-Long Tang
Weiyang Zhang
Qiao-Zhen Wang
Xin-Sheng Yao
Ping Dai
Kui Hong
Hao Gao
Chuan-Xi Wang
Source :
Acta Pharmaceutica Sinica. B, Acta Pharmaceutica Sinica B, Vol 11, Iss 2, Pp 588-597 (2021)
Publication Year :
2020
Publisher :
Elsevier, 2020.

Abstract

Organic carbonates (OCs) are a class of compounds featured by a carbonyl flanked by two alkoxy/aryloxy groups. They exist in either linear or cyclic forms, of which the majority encountered in nature adopt a pentacyclic structure. However, the enzymatic basis for pentacyclic carbonate ring formation remains elusive. Here, we reported that a four-protein metabolon (AlmUIIā€“UV) assembled by a small peptide protein (AlmUV) appends a reactive N-hydroxylcarbamoyl moiety to the decarboxylated aldgamycins followed by a non-enzymatic condensation to give the pentacyclic carbonate ring. Our results have documented an unprecedent mechanism for carbonate formation.<br />Graphical abstract The pentacyclic carbonate ring of aldgamycins is formed by a four-protein metabolon assembled by a small peptide protein, which begins with the attachment of a reactive N-hydroxylcarbamoyl moiety followed by a non-enzymatic condensation.Image 1

Details

Language :
English
ISSN :
22113843 and 22113835
Volume :
11
Issue :
2
Database :
OpenAIRE
Journal :
Acta Pharmaceutica Sinica. B
Accession number :
edsair.doi.dedup.....ef3b1f2a3281c5a8acce0f5a1cc55d76