Disease relevance of sulfanide

• To gain insight into the function of this enzyme at the atomic level, we have determined the first crystal structures of the 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8: holo enzyme and sulfate ion complex [1].
• Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes [2].
• We have determined the crystal structure of IMPDH from Borrelia burgdorferi, the bacterial spirochete that causes Lyme disease, with a sulfate ion bound in the IMP phosphate binding site [3].
• Male Swiss mice were subjected to CLP-induced sepsis and treated with saline (ip), dl-propargylglycine (PAG, 50 mg/kg ip), a CSE inhibitor, or sodium hydrosulfide (NaHS; 10 mg/kg ip) [4].
• However, the sulfate ion by itself does not inhibit the toxicity [5].

High impact information on sulfanide

• Interestingly, close to the PIF-pocket in PDK1, there is an ordered sulfate ion, interacting tightly with four surrounding side chains [6].
• The structure revealed the presence in the active site of a sulfate ion attached by an arginine clamp made by the side chain from two strictly conserved arginine residues [7].
• Previous x-ray crystallographic analysis of Zea mays PEPC has revealed a binding site for sulfate ion, speculated to be the site for an allosteric activator, glucose 6-phosphate (Glc-6-P) (Matsumura, H., Xie, Y., Shirakata, S., Inoue, T., Yoshinaga, T., Ueno, Y., Izui, K., and Kai, Y. (2002) Structure (Lond.) 10, 1721-1730) [8].
• Arrangement of substrates at the active site of yeast phosphoglycerate kinase. Effect of sulfate ion [9].
• Sulfate ion is not considered to be the physiological Fe2+-activator of P-enolpyruvate carboxykinase in rat liver cytosol, as this function is fulfilled by a newly discovered liver protein [10].

Chemical compound and disease context of sulfanide

• These results suggest that the replacement of chloride with sulfate ion suppresses the development of hypertension in DOCA-salt rats at least in part by its inhibitory effect on sympathetic nervous activity through the decreased intracellular calcium concentration [11].
• Here we report the crystal structure of DXR complexed with NADPH and a sulfate ion from Escherichia coli at 2.2 A resolution [12].
• Hydrosulfide anion did not appear to be an uncoupler of mitochondrial respiration in hepatocytes based upon the inability of oligomycin and fructose to protect hepatocytes from hydrosulfide anion toxicity [13].
• Comparing Escherichia coli and S. aureus CMK-CMP complex structures reveals differences within the active site, including a previously unreported indirect interaction of CMP with Asp33, the replacement of a serine residue involved in the binding of CDP by Ala12 in S. aureus CMK and an additional sulfate ion in the E. coli CMK active site [14].

Biological context of sulfanide

• Similarly, NMR studies showed that the environment of CrATP bound at the active site was altered by the presence of sulfate ion [9].
• A spectrophotometric determination of sulfate ion and its application in studies of substrate purity and of aryl sulfatase A kinetics [15].
• Arg41 from the other subunit enters the catalytic site and forms a hydrogen bond with a bound sulfate ion, an RNA main chain phosphate analog, thus activating its nucleophilic state [16].
• To evaluate the role of alternative mechanisms in H(2)S toxicity, the relative contributions of electron transport inhibition, uncoupling of mitochondrial respiration, and opening of the mitochondrial permeability transition pore (MPTP) to hydrosulfide and cyanide anion cytotoxicity in primary hepatocyte cultures were examined [13].
• The result show that the isolated A. terreus strain metabolises PAHs by reaction similar to those previously reported for non lignolinolytic fungi with a mechanism that suggests the hydroxylation by a cytochrome P-450 monooxygenase followed by conjugation with sulfate ion [17].

Anatomical context of sulfanide

• The CYS-14 protein appears to be localized in the plasma membrane, suggesting that it functions as a sulfate ion transporter [18].
• Activation energy of sulfate ion transport across methylated human erythrocyte membranes [19].
• The transport of sulfate ion across the endoplasmic reticulum membrane was investigated using rapid filtration and light scattering assays [20].
• Cytotoxic mechanisms of hydrosulfide anion and cyanide anion in primary rat hepatocyte cultures [13].
• Sodium and sulfate ion transport in yeast vacuoles [21].

Associations of sulfanide with other chemical compounds

• The model includes 303 residues, the flavin adenine dinucleotide cofactor (FAD), one sulfate ion located at the putative NADP+ binding site and 328 water molecule sites [22].
• In addition to interacting with the active site histidine, this sulfate ion is also hydrogen bonded to the guanidinium group of Arg-161, to the carboxamide group of Asn-140, and to the hydroxyl group of Ser-241 [23].
• The active site histidine, His-186, is hydrogen bonded from nitrogen ND1 to the carboxylate of Asp-158 and from its nitrogen NE2 to the sulfate ion bound in the putative substrate binding site [23].
• The finding of a sulfate ion binding site in the TAP structures, together with previous enzyme kinetic analyses, leads us to postulate that a putative CoA binding site is essential for efficient catalysis of thioesters in TAP [24].
• Here we report the crystal structure of human MAAI at 1.9 A resolution in complex with glutathione and a sulfate ion which mimics substrate binding [25].

Gene context of sulfanide

• Inhibition data of the cytosolic isozymes CA I and CA II as well as the membrane-bound isozyme CA IV with a large number of anionic species such as halides, pseudohalides, bicarbonate, nitrate, hydrosulfide, arsenate, sulfamate, and sulfamidate and so on, are also provided for comparison [26].
• The structure of MTAP with methylthioadenosine and sulfate ion soaked into the active site was also determined using diffraction data to 1.7 A resolution [27].
• 4. Sulfate ion caused 3-fold activation of aldose reductase, but little for that of aldehyde reductase [28].
• The inhibitor only partially mimics the RNase-nucleotide interaction and does not utilize the p1 phosphate-binding pocket of ribonuclease A, where a sulfate ion remains bound [29].
• The hydrogen bond with the N delta 2 moiety of Asn 18 appears to be the most conserved interaction, being similar to those observed for sulfate ion bound to human basic FGF (bFGF) and similar but not identical to interactions observed for bovine aFGF with heparin analogs [30].

Analytical, diagnostic and therapeutic context of sulfanide

• Sodium hydrosulfide (NaHS) was given by intraperitoneal injection to both the control group and the l-NAME-treated group [31].
• In continuation of earlier work [Hu, C. Q., & Sturtevant, J.M. (1987) Biochemistry 26, 178-182], differential scanning calorimetry has been employed in a study of the effects on the thermal denaturation of yeast phosphoglycerate kinase of two inhibitors of the enzyme, sulfate ion and the dye Cibracron blue F3GA [32].
• An enzyme electrode based on immobilized arylsulfatase for the selective assay of sulfate ion [33].
• A sulfate ion from the crystallization buffer is also trapped in the B helix between the guanidinium group of Arg47 and these two inserted water molecules [34].
• The dodecyl sulfate ion selective electrode (EMF), isothermal titration calorimetry (ITC), and surface tension (ST) were applied to gain detailed information about interactions [35].

References