Next Article in Journal
Synthetic Evaluation of Standard and Microwave-Assisted Solid Phase Peptide Synthesis of a Long Chimeric Peptide Derived from Four Plasmodium falciparum Proteins
Previous Article in Journal
Preparation of Functional Monomers as Precursors of Bioprobes from a Common Styrene Derivative and Polymer Synthesis
Article Menu

Export Article

Open AccessArticle
Molecules 2018, 23(11), 2876;

Biochemical and Functional Characterization of Anthocyanidin Reductase (ANR) from Mangifera indica L.

Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences (CATAS)—Hainan Key Laboratory of Banana Genetic Improvement, Haikou 570102, Hainan Province, China
National Center for Natural Products Research, Thad Cochran Research Center, School of Pharmacy, University of Mississippi, University, MS 38677, USA
Department of Basic Education in Liberal Arts, Hainan University, Haikou 571101, Hainan Province, China
Department of Bioinformatics and Biotechnology, Government College University, Faisalabad 38000, Pakistan
Institute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural Sciences (CATAS), Haikou 571101, Hainan Province, China
Programa Ofidismo-Escorpionismo, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia, Medellín 1226, Colombia
United States Department of Agriculture, Agricultural Research Service, Natural Products Utilization Research Unit (USDA-ARS-NPURU), P.O. Box 1848, University, MS 38677-1848, USA
Author to whom correspondence should be addressed.
Received: 30 September 2018 / Revised: 27 October 2018 / Accepted: 30 October 2018 / Published: 5 November 2018
Full-Text   |   PDF [4205 KB, uploaded 5 November 2018]   |  


Mango (Mangifera indica L.) is abundant in proanthocyanidins (PAs) that are important for human health and plant response to abiotic stresses. However, the molecular mechanisms involved in PA biosynthesis still need to be elucidated. Anthocyanidin reductase (ANR) catalyzes a key step in PA biosynthesis. In this study, three ANR cDNAs (MiANR1-1,1-2,1-3) were isolated from mango, and expressed in Escherichia coli. In vitro enzyme assay showed MiANR proteins convert cyanidin to their corresponding flavan-3-ols, such as (−)-catechin and (−)-epicatechin. Despite high amino acid similarity, the recombinant ANR proteins exhibited differences in enzyme kinetics and cosubstrate preference. MiANR1-2 and MiANR1-3 have the same optimum pH of 4.0 in citrate buffer, while the optimum pH for MiANR1-1 is pH 3.0 in phosphate buffer. MiANR1-1 does not use either NADPH or NADH as co-substrate while MiANR1-2/1-3 use only NADPH as co-substrate. MiANR1-2 has the highest Km and Vmax for cyanidin, followed by MiANR1-3 and MiANR1-1. The overexpression of MiANRs in ban mutant reconstructed the biosynthetic pathway of PAs in the seed coat. These data demonstrate MiANRs can form the ANR pathway, leading to the formation of two types of isomeric flavan-3-ols and PAs in mango. View Full-Text
Keywords: anthocyanidin reductase; (−)-epicatechin; (−)-catechin; proanthocyanidins; Mangifera indica L. anthocyanidin reductase; (−)-epicatechin; (−)-catechin; proanthocyanidins; Mangifera indica L.

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Tan, L.; Wang, M.; Kang, Y.; Azeem, F.; Zhou, Z.; Tuo, D.; María Preciado Rojo, L.; Khan, I.A.; Pan, Z. Biochemical and Functional Characterization of Anthocyanidin Reductase (ANR) from Mangifera indica L.. Molecules 2018, 23, 2876.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top