4756-85-8Relevant articles and documents
Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism
Irani, Seema,Naowarojna, Nathchar,Tang, Yang,Kathuria, Karan R.,Wang, Shu,Dhembi, Anxhela,Lee, Norman,Yan, Wupeng,Lyu, Huijue,Costello, Catherine E.,Liu, Pinghua,Zhang, Yan Jessie
, p. 519 - 4,529 (2018)
Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent pyridoxal 5′-phosphate (PLP)-mediated C-S lyase reaction leads to the net transfer of a sulfur atom from a cysteine to a histidine. In this study, we structurally and mechanistically characterized a PLP-dependent C-S lyase Egt2, which mediates the sulfoxide C-S bond cleavage in ergothioneine biosynthesis. A cation-π interaction between substrate and enzyme accounts for Egt2's preference of sulfoxide over thioether as a substrate. Using mutagenesis and structural biology, we captured three distinct states of the Egt2 C-S lyase reaction cycle, including a labile sulfenic intermediate captured in Egt2 crystals. Chemical trapping and high-resolution mass spectrometry were used to confirm the involvement of the sulfenic acid intermediate in Egt2 catalysis. Irani et al. have determined the structure of Egt2, a C-S lyase at the final step in the ergothioneine biosynthesis pathways. Using X-ray crystallography and various biochemical studies, the reaction mechanism was delineated.
Biosynthesis of ergothioneine by Claviceps purpurea. II. Incorporation of [35S]methionine and the non-utilization of [2(ring)-14C]histamine.
WILDY,HEATH
, p. 220 - 222 (1957)
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In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions
Naowarojna, Nathchar,Huang, Pei,Cai, Yujuan,Song, Heng,Wu, Lian,Cheng, Ronghai,Li, Yan,Wang, Shu,Lyu, Huijue,Zhang, Lixin,Zhou, Jiahai,Liu, Pinghua
, p. 5427 - 5430 (2018/09/12)
Ovothiols are thiolhistidine derivatives. The first step of ovothiol biosynthesis is OvoA-catalyzed oxidative coupling between histidine and cysteine. In this report, the remaining steps of ovothiol A biosynthesis were reconstituted in vitro. ETA-14770 (OvoB) was reported as a PLP-dependent sulfoxide lyase, responsible for mercaptohistidine production. OvoA was found to be a bifunctional enzyme, which mediates both oxidative C-S bond formation and methylation of mercaptohistidine to afford ovothiol A. Besides reconstituting the whole biosynthetic pathway, two unique features proposed in the literature were also examined: A potential cysteine-recycling mechanism of the C-S lyase (OvoB) and the selectivity of the ?-N methyltransferase.
Cysteine as a sustainable sulfur reagent for the protecting-group-free synthesis of sulfur-containing amino acids: Biomimetic synthesis of l-ergothioneine in water
Erdelmeier, Irene,Daunay, Sylvain,Lebel, Remi,Farescour, Laurence,Yadan, Jean-Claude
supporting information; scheme or table, p. 2256 - 2265 (2012/09/08)
Biomass-derived cysteine was used as a sustainable sulfur source for the synthesis of rare sulfur-containing amino acids, such as l-ergothioneine (4), which might be a new vitamin, and various l- or d-2-thiohistidine compounds. Key in this simple, one-pot two-step procedure in water is a bromine-induced regioselective introduction of cysteine followed by a novel thermal cleavage reaction in the presence of thiols, a safer alternative to hazardous red phosphorus. Besides avoiding hazardous sulfur reagents, the new protecting-group-free approach reduces drastically the total number of steps, compared to described procedures. The main drawback, i.e. handling of liquid bromine as an activating and oxidizing reagent in water, was addressed by evaluating four alternative methods using in situ generation of bromine or HOBr, and first encouraging results are described.
