3,4-Dihydroxyphenylacetaldehyde synthase evolved an ordered structure to deliver oxygen to pyridoxal 5’-phosphate for cuticle assembly in the mosquito Aedes aegypti

Jing Chen, Christopher J. Vavricka (), Shuangshuang Wei, Yasumoto Nakazawa, Yuri Matsumoto, Huaqing Chen, Yu Tang, Jing Liang, Jiukai Chen, Yaneng Huang, Keiichi Noguchi, Tomohisa Hasunuma, Huai Guan, Jianyong Li, Chenghong Liao () and Qian Han ()
Additional contact information
Jing Chen: Hainan University
Christopher J. Vavricka: Koganei
Shuangshuang Wei: Hainan University
Yasumoto Nakazawa: Koganei
Yuri Matsumoto: Koganei
Huaqing Chen: Hainan University
Yu Tang: Hainan University
Jing Liang: Virginia Polytechnic Institute and State University
Jiukai Chen: Hainan University
Yaneng Huang: Hainan University
Keiichi Noguchi: Koganei
Tomohisa Hasunuma: Kobe University
Huai Guan: Hainan University
Jianyong Li: Virginia Polytechnic Institute and State University
Chenghong Liao: Hainan University
Qian Han: Hainan University

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract 3,4-Dihydroxyphenylacetaldehyde synthase (DHPAAS) catalyzes oxygen-dependent conversion of 3,4-dihydroxyphenylalanine (dopa) to 3,4-dihydroxyphenylacetaldehyde (DHPAA), a likely cross-linking agent precursor of the insect cuticle. In the current study, extensive in vivo experiments in Aedes aegypti show that DHPAAS is essential for abdominal integrity, egg development and cuticle structure formation. Solid-state 13C nuclear magnetic resonance analysis of the Ae. aegypti cuticle molecular structure shows chemical shifts of 115 to 145 ppm, suggesting the presence of catechols derived from DHPAA. The crystal structure of insect DHPAAS was then solved, revealing an active site that is divergent from that of the homologous enzyme dopa decarboxylase. In the DHPAAS crystal structure, stabilization of the flexible 320–350 region accompanies the positioning of the 350–360 loop relatively close to the catalytic Asn192 residue while the conserved active site residue Phe103 adopts an open conformation away from the active center; these distinct features participate in the formation of a specific hydrophobic tunnel which potentially facilitates delivery of oxygen to pyridoxal 5’-phosphate in the conversion of dopa to DHPAA.

Date: 2025
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DOI: 10.1038/s41467-025-59723-0

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