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• W2009554939 abstract "Human cystathionine β-synthase (CBS), a novel heme-containing pyridoxal 5′-phosphate enzyme, catalyzes the condensation of homocysteine and serine or cysteine to produce cystathionine and H2O or H2S, respectively. The presence of heme in CBS has limited spectrophotometric characterization of reaction intermediates by masking the absorption of the pyridoxal 5′-phosphate cofactor. In this study, we employed difference stopped-flow spectroscopy to characterize reaction intermediates formed under catalytic turnover conditions. The reactions of l-serine and l-cysteine with CBS resulted in the formation of a common aminoacrylate intermediate (kobs = 0.96 ± 0.02 and 0.38 ± 0.01 mm−1 s−1, respectively, at 24 °C) with concomitant loss of H2O and H2S and without detectable accumulation of the external aldimine or other intermediates. Homocysteine reacted with the aminoacrylate intermediate with kobs = 40.6 ± 3.8 s−1 and re-formed the internal aldimine. In the reverse direction, CBS reacted with cystathionine, forming the aminoacrylate intermediate with kobs = 0.38 ± 0.01 mm−1 s−1. This study provides the first insights into the pre-steady-state kinetic mechanism of human CBS and indicates that the reaction is likely to be limited by a conformational change leading to product release. Human cystathionine β-synthase (CBS), a novel heme-containing pyridoxal 5′-phosphate enzyme, catalyzes the condensation of homocysteine and serine or cysteine to produce cystathionine and H2O or H2S, respectively. The presence of heme in CBS has limited spectrophotometric characterization of reaction intermediates by masking the absorption of the pyridoxal 5′-phosphate cofactor. In this study, we employed difference stopped-flow spectroscopy to characterize reaction intermediates formed under catalytic turnover conditions. The reactions of l-serine and l-cysteine with CBS resulted in the formation of a common aminoacrylate intermediate (kobs = 0.96 ± 0.02 and 0.38 ± 0.01 mm−1 s−1, respectively, at 24 °C) with concomitant loss of H2O and H2S and without detectable accumulation of the external aldimine or other intermediates. Homocysteine reacted with the aminoacrylate intermediate with kobs = 40.6 ± 3.8 s−1 and re-formed the internal aldimine. In the reverse direction, CBS reacted with cystathionine, forming the aminoacrylate intermediate with kobs = 0.38 ± 0.01 mm−1 s−1. This study provides the first insights into the pre-steady-state kinetic mechanism of human CBS and indicates that the reaction is likely to be limited by a conformational change leading to product release." @default.
• W2009554939 created "2016-06-24" @default.
• W2009554939 creator A5013907641 @default.
• W2009554939 creator A5040682203 @default.
• W2009554939 date "2012-12-01" @default.
• W2009554939 modified "2023-10-08" @default.
• W2009554939 title "Detection of Reaction Intermediates during Human Cystathionine β-Synthase-monitored Turnover and H2S Production" @default.
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• W2009554939 doi "https://doi.org/10.1074/jbc.m112.414722" @default.
• W2009554939 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3527933" @default.
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