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. 2024 Aug 8;15(1):6715.
doi: 10.1038/s41467-024-50703-4.

LsBOS utilizes oxalyl-CoA produced by LsAAE3 to synthesize β-ODAP in grass pea

Affiliations

LsBOS utilizes oxalyl-CoA produced by LsAAE3 to synthesize β-ODAP in grass pea

Moshe Goldsmith et al. Nat Commun. .
No abstract available

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1. Synthesis of β-ODAP from oxalyl-CoA and L-DAPA by LsBOS.
Purified oxalyl-CoA (0.4 mM) was incubated with L-DAPA (0.4 mM) and LsBOS (0.15 μM) for 1 h at 37 °C at pH 7.5 (complete reaction). Similar reaction mixtures containing either: no enzyme (No Enz) or with LsAAE3 (0.15 μM) replacing LsBOS (LsAAE3) at pH 7.5 or pH 9 were similarly incubated for 1 h at 37 °C. A control reaction containing only LsAAE3 (0.15μM) and oxalyl-CoA (0.4 mM) at pH 7.5 (LsAAE3 + oxalyl-CoA) was similarly incubated. The reactions were inactivated, diluted 1:10, and the amount of β-ODAP product was quantified in each reaction using LC-MS. Source data are provided as a Source Data file.
Fig. 2
Fig. 2. Kinetics of oxalate ligation to CoA by LsAAE3 with and without L-DAPA.
The rates of CoA (2 mM) ligation to oxalate (0.5 mM) were assayed at pH 7.5 using purified LsAAE3 (1μM) in the presence of ATP (5 mM) and Mg+2 (5 mM; blue bar) and with the addition of L-DAPA (3 mM; red bar). Initial reaction rates were determined using an NADH-coupled enzymatic assay. Error bars denote the SD of four independent replicates (n = 4). Data was analyzed using a two-tailed t-test. ns – not significant (p ≥ 0.05). Source data are provided as a Source Data file.

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References

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