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- W2474895874 abstract "Abstract We have conducted biochemical studies with commercial available pyrroline‐5‐carboxylate (P5C) reductase (PYCR1) to investigate whether this enzyme plays a role in L‐lysine degradation. Our recent studies with antiquitin/ALDH7A1 deficient fibroblasts revealed an alternative genesis of L‐pipecolic acid, and we then hypothesized that PYCR1 was responsible for the conversion of Δ 1 ‐piperideine‐6‐carboxylate (P6C) into pipecolic acid. We here present evidence that PYCR1 is indeed able to produce L‐pipecolic acid from P6C preparations, and the observed K m for this conversion is of the same magnitude as the K m described for the conversion of P5C to L‐proline by PYCR1. Urine samples from antiquitin deficient individuals, who accumulate P6C, were also incubated with PYCR1 which resulted in a marked decrease of P6C and a huge increase of L‐pipecolic acid as measured by LC‐MS/MS, confirming that indeed PYCR1 generates L‐pipecolic acid from P6C." @default.
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- W2474895874 date "2014-01-16" @default.
- W2474895874 modified "2023-10-16" @default.
- W2474895874 title "Human pyrroline-5-carboxylate reductase (PYCR1) acts on Δ1-piperideine-6-carboxylate generating L-pipecolic acid" @default.
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- W2474895874 doi "https://doi.org/10.1007/s10545-013-9673-4" @default.
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