Disease relevance of NSC 32950

• Evidence for an essential arginine residue in the active site of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. Modification with 1,2-cyclohexanedione [1].
• Fragmentations of the CN peptides were accomplished by digestions with trypsin (after citraconylation or 1,2-cyclohexanedione treatment), chymotrypsin and Staphylococcus aureus external protease [2].
• Inhibition of Clostridium difficile toxin A and B by 1,2-cyclohexanedione modification of an arginine residue [3].
• Modification of the guanidine side chain of Arg-13 with both 1,2-cyclohexanedione and phenylglyoxal decreased the toxicity of RTX-III by a factor of five [4].

High impact information on NSC 32950

• Binding of LDL to the granules was essential for the granule-mediated uptake of LDL by macrophages, for the uptake process was prevented by treating the granules with avidin or protamine chloride or by treating LDL with 1,2-cyclohexanedione, all of which inhibit the binding of LDL to the granules [5].
• Modification of arginine-198 in sarcoplasmic reticulum Ca2+-ATPase by 1,2-cyclohexanedione causes inhibition of formation of the phosphoenzyme intermediate from inorganic phosphate [6].
• The inhibitory effect of apoE was not abolished by reductive methylation of lysine residues, whereas selective modification of arginine residues by 1,2-cyclohexadione completely cancelled the inhibitory effect of apoE [7].
• The immunoglobulin G binding site in the globular regions of human complement subcomponent C1q has been investigated by chemical modification of histidine residues with diethylpyrocarbonate and arginine residues with phenylglyoxal and cyclohexane-1,2-dione (CHD) [8].
• The role of arginine residues on lactoferrin was studied by modifying these residues with 1,2-cyclohexanedione [9].

Biological context of NSC 32950

• Identification of arginyl residues located at the ATP binding site of sarcoplasmic reticulum Ca2+-ATPase. Modification with 1,2-cyclohexanedione [10].
• Conversely, this binding was decreased with proteolytic fragmentation of IgG, high ionic strength (at pH above 4), or temperatures above 4 degrees C. Chemical modification of IgG by acetylation, formalinization, carbamylation, or reaction with 1,2-cyclohexanedione significantly decreased these interactions [11].
• Reaction of 1,2-cyclohexanedione with kringle 1 was found to rapidly abolish the fibrin-Sepharose affinity of the fragment, whereas the affinity for lysine-Sepharose was lost at a significantly slower rate [12].
• The flavoenzyme pig kidney general acyl-CoA dehydrogenase (EC 1.3.99.3) is inactivated by cyclohexane-1,2-dione in borate buffer in a reaction that exhibits pseudo-first-order kinetics [13].
• The complete amino acid sequence of the alpha chain of the dimeric sarcoplasmic Ca2+-binding protein (SCP-I = alpha 2) from crayfish (Astacus leptodactylus) has been determined by partial automatic sequencing of the peptides derived from tryptic digests of the protein after citraconylation or treatment with 1,2-cyclohexanedione [14].

Anatomical context of NSC 32950

• 1,2-Cyclohexanedione modification of human LDL abolishes its recognition by high affinity cell membrane receptors in vitro and delays its plasma clearance in comparison to native LDL [15].
• The utility of 1,2 cyclohexanedione-modified low density lipoprotein (CHD-LDL) as a marker for the measurement of receptor independent LDL catabolism has been assessed by examining its metabolic properties in cultured human fibroblasts and in rabbits [16].
• Binding of human low density lipoproteins (LDL) to their specific receptor on cultured cells can be inhibited by treatment with 1,2-cyclohexanedione which blocks a number of functionally significant arginyl residues on the apolipoprotein [17].
• After modification of its arginine side chains by exposure to 1,2-cyclohexanedione (CHD) in the presence of 0.2 M-NaOH, BSA lost its property of reducing Lp in capillaries perfused with Ringer solution [18].
• Inhibition of anion transport across red blood cells with 1,2-cyclohexanedione [19].

Associations of NSC 32950 with other chemical compounds

• The binding of CNBr II . DMPC was inhibited by 1,2-cyclohexanedione modification of arginyl residues or diketene modification of lysyl residues [20].
• Chemical modification by pyridoxal 5'-phosphate and cyclohexane-1,2-dione indicates that Lys-7 and Arg-10 are involved in the p2 phosphate-binding subsite of bovine pancreatic ribonuclease A [21].
• While Aspergillus ficuum phytaseA (phyA) was rapidly inactivated by 1,2-cyclohexanedione and phenylglyoxal, both specific modifiers of arginine, phytaseB (phyB) showed a markedly different behavior [22].
• The (R)-enzyme was most active at pH 6.4 and accepted in addition to diacetyl C5-, C6-2,3-diketones, 1,2-cyclohexanedione, 2-oxo aldehydes and short-chain 2- and 3-oxo esters as substrates [23].
• Novel biscapped and monocapped tris(dioxime) Mn(II) complexes: x-ray crystal structure of the first cationic tris(dioxime) Mn(II) complex [Mn(CDOH)3BPh]OH (CDOH2= 1,2-cyclohexanedione dioxime) [24].

Gene context of NSC 32950

• Modification of apolipoprotein C-II with 1,2-cyclohexanedione and 2,3-butanedione. Role of arginine in the activation of lipoprotein lipase [25].
• Human argininosuccinate synthetase (ASS) activity was found to be inactivated by alpha-dicarbonyls such as 1,2-cyclohexanedione and phenylglyoxal in accordance with pseudo first-order kinetics [26].
• Furthermore, unlabeled 1,2-cyclohexanedione-modified lactoferrin did not inhibit the binding of 125I-lactoferrin to isolated parenchymal cells [9].
• D-Amino acid oxidase is inactivated by reaction with 1,2-cyclohexanedione in borate buffer at pH 8 [27].
• ADP-ribosylation did not affect the stimulation while the 1,2-cyclohexanedione modified MBP and the peptidylarginine deiminase-treated MBP showed a reduced ability to stimulate the PI-PLC activity which correlated with the number of arginyl residues modified [28].

Analytical, diagnostic and therapeutic context of NSC 32950

• X-ray photoelectron spectroscopy (XPS) and Fourier transform infrared spectroscopy (FTIR) are used to compare the reaction of 1,2-cyclohexanedione (1,2-CHD) with Si(001) and diamond(001) surface dimers under ultra-high-vacuum conditions [29].
• Evidence is given by NMR, UV, and titration data that a complex is formed from 1,2-cyclohexanedione and borate [30].

References