Enzymes
UniProtKB help_outline | 4 proteins |
GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKeyhelp_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ethanolamine Identifier CHEBI:57603 Charge 1 Formula C2H8NO InChIKeyhelp_outline HZAXFHJVJLSVMW-UHFFFAOYSA-O SMILEShelp_outline [NH3+]CCO 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,032 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:45824 | RHEA:45825 | RHEA:45826 | RHEA:45827 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Plants synthesize ethanolamine by direct decarboxylation of serine using a pyridoxal phosphate enzyme.
Rontein D., Nishida I., Tashiro G., Yoshioka K., Wu W.I., Voelker D.R., Basset G., Hanson A.D.
The established pathways from serine to ethanolamine are indirect and involve decarboxylation of phosphatidylserine. Here we show that plants can decarboxylate serine directly. Using a radioassay based on ethanolamine (Etn) formation, pyridoxal 5'-phosphate-dependent l-serine decarboxylase (SDC) a ... >> More
The established pathways from serine to ethanolamine are indirect and involve decarboxylation of phosphatidylserine. Here we show that plants can decarboxylate serine directly. Using a radioassay based on ethanolamine (Etn) formation, pyridoxal 5'-phosphate-dependent l-serine decarboxylase (SDC) activity was readily detected in soluble extracts from leaves of diverse species, including spinach, Arabidopsis, and rapeseed. A putative Arabidopsis SDC cDNA was identified by searching GenBank for sequences homologous to other amino acid decarboxylases and shown by expression in Escherichia coli to encode a soluble protein with SDC activity. This cDNA was further authenticated by complementing the Etn requirement of a yeast psd1 psd2 mutant. In a parallel approach, a cDNA was isolated from a rapeseed library by its ability to complement the Etn requirement of a yeast cho1 mutant and shown by expression in E. coli to specify SDC. The deduced Arabidopsis and rapeseed SDC polypeptides are 90% identical, lack obvious targeting signals, and belong to amino acid decarboxylase group II. Recombinant Arabidopsis SDC was shown to exist as a tetramer and to contain pyridoxal 5'-phosphate. It does not attack d-serine, l-phosphoserine, other l-amino acids, or phosphatidylserine and is not inhibited by Etn, choline, or their phosphoesters. As a soluble, pyridoxal 5'-phosphate enzyme, SDC contrasts sharply with phosphatidylserine decarboxylases, which are membrane proteins that have a pyruvoyl cofactor. << Less
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Structure and evolution of alanine/serine decarboxylases and the engineering of theanine production.
Wang H., Zhu B., Qiao S., Dong C., Wan X., Gong W., Zhang Z.
Ethylamine (EA), the precursor of theanine biosynthesis, is synthesized from alanine decarboxylation by alanine decarboxylase (AlaDC) in tea plants. AlaDC evolves from serine decarboxylase (SerDC) through neofunctionalization and has lower catalytic activity. However, lacking structure information ... >> More
Ethylamine (EA), the precursor of theanine biosynthesis, is synthesized from alanine decarboxylation by alanine decarboxylase (AlaDC) in tea plants. AlaDC evolves from serine decarboxylase (SerDC) through neofunctionalization and has lower catalytic activity. However, lacking structure information hinders the understanding of the evolution of substrate specificity and catalytic activity. In this study, we solved the X-ray crystal structures of AlaDC from <i>Camellia sinensis</i> (CsAlaDC) and SerDC from <i>Arabidopsis thaliana</i> (AtSerDC). Tyr<sup>341</sup> of AtSerDC or the corresponding Tyr<sup>336</sup> of CsAlaDC is essential for their enzymatic activity. Tyr<sup>111</sup> of AtSerDC and the corresponding Phe<sup>106</sup> of CsAlaDC determine their substrate specificity. Both CsAlaDC and AtSerDC have a distinctive zinc finger and have not been identified in any other Group II PLP-dependent amino acid decarboxylases. Based on the structural comparisons, we conducted a mutation screen of CsAlaDC. The results indicated that the mutation of L110F or P114A in the CsAlaDC dimerization interface significantly improved the catalytic activity by 110% and 59%, respectively. Combining a double mutant of CsAlaDC<sup>L110F/P114A</sup> with theanine synthetase increased theanine production 672% in an <i>in vitro</i> system. This study provides the structural basis for the substrate selectivity and catalytic activity of CsAlaDC and AtSerDC and provides a route to more efficient biosynthesis of theanine. << Less
Elife 12:RP91046-RP91046(2024) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.