The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN)

Stephen A. Marshall; Karl A.P. Payne; David Leys

doi:10.1016/j.abb.2017.07.014

The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN)

Stephen A. Marshall, Karl A.P. Payne, David Leys^*

^*Corresponding author for this work

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Abstract

The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.

Original language	English
Journal	Archives of Biochemistry and Biophysics
Early online date	25 Jul 2017
DOIs	https://doi.org/10.1016/j.abb.2017.07.014
Publication status	Published - 2017

Keywords

(de)Carboxylase
Cycloaddition
Prenyl transferase
Prenylated FMN
UbiD
UbiX

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10.1016/j.abb.2017.07.014

ABB_revised (2)Accepted author manuscript, 24.2 MB

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title = "The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN)",

abstract = "The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.",

keywords = "(de)Carboxylase, Cycloaddition, Prenyl transferase, Prenylated FMN, UbiD, UbiX",

author = "Marshall, {Stephen A.} and Payne, {Karl A.P.} and David Leys",

year = "2017",

doi = "10.1016/j.abb.2017.07.014",

language = "English",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

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T1 - The UbiX-UbiD system

T2 - The biosynthesis and use of prenylated flavin (prFMN)

AU - Marshall, Stephen A.

AU - Payne, Karl A.P.

AU - Leys, David

PY - 2017

Y1 - 2017

N2 - The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.

AB - The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.

KW - (de)Carboxylase

KW - Cycloaddition

KW - Prenyl transferase

KW - Prenylated FMN

KW - UbiD

KW - UbiX

UR - http://www.scopus.com/inward/record.url?scp=85026785223&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2017.07.014

DO - 10.1016/j.abb.2017.07.014

M3 - Article

AN - SCOPUS:85026785223

SN - 0003-9861

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

ER -

The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN)

Abstract

Keywords

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