Fig. 1: Structure and function of DHAD and its catalytic mechanism. | Nature Communications

Fig. 1: Structure and function of DHAD and its catalytic mechanism.

From: Substrate-based discovery of α-hydroxycarboxylic acid derivatives as potential herbicides targeting dihydroxyacid dehydratase

Fig. 1: Structure and function of DHAD and its catalytic mechanism.

a Branched-chain amino acid biosynthetic pathway. b Amino acid sequence alignment of DHADs from Arabidopsis thaliana (AtDHAD, 5ZE4), Spinacia oleracea (SoDHAD, XP_021849033.1), Synechocystis sp. PCC 6803 (SnDHAD, 6NTE), Mycobacterium tuberculosis (MtbDHAD, 6OVT) and Escherichia coli (EcDHAD, ACX41805.1). The truncated sequences primarily display key amino acid residues within the catalytic active site of the protein. c Superposition of the three-dimensional structures of AtDHAD and MtbDHAD and residues in the active pocket. d Superposition of the three-dimensional structures of AtDHAD–AA (9JPI) and AtDHAD (5ZE4). Conformational changes in amino acid residues in the active pocket.

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