CAS: 2686-70-6; (2S)-2-Amino-4-Sulfinobutanoic Acid

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L-高半胱氨酸 L-Homocysteine 6027-13-0

📜L-高半胱氨酸置于cysteine Dioxygenase,Sodium Chloride体系中,用 Aq. Phosphate Buffer,重水 用作溶剂,化学反应 0.03H,反应生成L-高半胱氨酸亚磺酸
参考文献:Steady-State Substrate Specificity And O2-Coupling Efficiency Of Mouse Cysteine Dioxygenase
标题:Steady-State Substrate Specificity And O2-Coupling Efficiency Of Mouse Cysteine Dioxygenase
摘要:Cysteine Dioxygenase (Cdo) Is A Non-Heme Mononuclear Iron Enzyme That Catalyzes The Oxygendependent Oxidation Of L-Cysteine (Cys) To Produce L-Cysteine Sulfinic Acid (Csa). Sequence Alignment Of Mammalian Coo With Recently Discovered Thiol Dioxygenase Enzymes Suggests That The Mononuclear Iron Site Within All Enzymes In This Class Share A Common 3-His First Coordination Sphere. This Implies A Similar Mechanistic Paradigm Among Thiol Dioxygenase Enzymes. Although Steady-State Studies Were First Reported For Mammalian Cdo Over 45 Years Ago,Detailed Analysis Of The Specificity For Alternative Thiol-Bearing Substrates And Their Oxidative Coupling Efficiencies Have Not Been Reported For This Enzyme. Assuming A Similar Mechanistic Theme Among This Class Of Enzymes,Characterization Of The Cdo Substrate Specificity May Provide Valuable Insight Into Substrate-Active Site Intermolecular During Thiol Oxidation. In This Work,The Substrate-Specificity For Wild-Type Mus Musculus Cdo Was Investigated Using NMR Spectroscopy And Lc-Ms For A Variety Of Thiol-Bearing Substrates. Tandem Mass Spectrometry Was Used To Confirm Dioxygenase Activity For Each Non-Native Substrate Investigated. Steady-State Michaelismenten Parameters For Sulfinic Acid Product Formation And O-2-Consumption Were Compared To Establish The Coupling Efficiency For Each Reaction. In Light Of These Results,The Minimal Substrate Requirements For Cdo Catalysis And O-2-Activation Are Discussed. (C) 2014 Elsevier Inc. All Rights Reserved.
Doi:10.1016/j.Abb.2014.11.004