Introduction of the cyano group into the molecule

Friedrich, K.; Wallenfels, Kurt

doi:10.1002/9780470771242.ch2

Cited by 56 publications

(33 citation statements)

References 267 publications

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“…The effects of metabolic inhibitors also depended on the carbon source used for growth: in cells grown on glucose, both KCN and dinitrophenol stimulated the initial MeClc uptake rate by themselves, but only KCN increased steady-state uptake levels as well 19,101. With lactate as carbon source, both initial rate and steady-state uptake were decreased by KCN, whereas dinitrophenol stimulated the initial uptake rate and did not affect steady-state accumulation [9, 101.…”

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confidence: 99%

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Rohwer

Jensen

Shinohara

et al. 1996

European Journal of Biochemistry

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The effect of different cellular free-energy states on the uptake of methyl G-D-glucopyranoSide, an analogue of glucose, by the Escherichia coli phosphoennlpyruvate :carbohydrate phosphotransferase system was investigated. The intracellular IATP]/[ADP] ratio was varied by changing the expression of the atp operon, which codes for the Hi-ATPase, or by adding an uncoupler of oxidative phosphorylation or an inhibitor of respiration. Corresponding initial phosphotransferase uptake rates were determined using an improved uptake assay that works with growing cells in steady state. Escheuichia coli can use any one of a large variety of compounds as the sole carbon source for growth. In the presence of a mixture of compounds, this bacterium will often show a preference for certain carbohydrates, such as glucose, and repress the expression of uptake systems for other compounds (inducer exclusion [I I). During growth on a different carbon source such as succinate, however, E. coli maintains a relatively high capacity for glucosc transport [I 1. The bacterial phosphoenolpyruvate : carbohydratc phosphotransferase system catalyses the uptake and concomitant phosphorylation of a variety of carbohydratcs, for example glucose 11 1. The phosphotransferase system is a group-transfer pathway consisting of two soluble phosphoproteins (Enzyme 1 and HPr) and, for each carbohydrate, a specil'ic protein or protein complex, the carbohydrate permease (for E. r d i in the case of glucose, soluble Enzyme IIA"" and membrane-bound Enzyme IICB""). During the uptake of a glucose moleculc, for example, a phosphoryl group from phosphoenol- Ahhvevi~ition.~. Phosphotransferase system, phosphoenolpyruvate :carbohydrate phosphotransferase system; HPr, histidine-containing protein; Enzyme I, phosphoenolpyruvate-protein phosphotransferase; Enryme 11, prolein-N"-phosphohistidine-sugar phosphotransferase; IIA"" and IICB"", EnLyines 11 of thc phosphoenolpyruvatc: glucose pliosphotransicrasc system; MeGlc, methyl cr-D-glucopyranoside; IPTG, isopropyl tliio-Pi,-galactoside. Enzsmc,.s. EnLyme 1 of the phosphotransferase system, phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9); Enzyme I1 of the phosphotransferase system, protein-N"-phosphohistidine-sugar phosphotransferasc (EC 2.7.1.69).pyruvate is transferred sequentially along Enzyme 1, HPr, Enzymes IIAG1" and IICB"", to the glucose molecule.Metabolic activity and changes in the cellular energy state have been shown to affect phosphotransferase activity in a variety of ways: the addition of substrates to activate respiration reduced the steady-state accumulation of methyl am-glucopyranoside (MeGlc) 12, 31, a non-metabolisable analogue of the glucose phosphotransferase system; the inhibition of MeGlc uptake by respiration was more severe in atp mutants, which cannot use the protonmotive force to synthesise ATP 141 ; the inhibition by oxidisable substrates could be reversed by the addition of uncouplers of oxidative phosphorylation such as carbonyl cyanide rnchlorophenylhydrazone [2) or 2,4-dinitr...

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confidence: 99%

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Rohwer

Jensen

Shinohara

et al. 1996

European Journal of Biochemistry

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“…3 Aryl nitriles have been prepared by cyanation of iodides or bromides using CuCN or KCN in absence of solvent or in solvents like pyridine, quinoline, DMF, NMP at elevated temperature. [4][5][6][7][8][9][10][11] Under Von Braun conditions the reaction of 5-bromo-2-methoxypyrimidine with [ 14 C] CuCN in DMF at 1451C for 48 h did not yield cyano derivative.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of [¹⁴C] labeled 2‐methoxypyrimidine‐5‐carboxylic acid

Murthy¹,

Ullas²

2009

Labelled Comp Radiopharmac

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“…Cyanohydrins, also called ␣-hydroxynitriles, are organic cyanides with the general structure R 1 R 2 C(OH)(CN), where the hydroxide group and cyanide group are attached to the same carbon atom. According to Friedrich and Wallenfels (1970), cyanohydrins can release cyanide on hydrolysis as follows:…”

Section: Introductionmentioning

confidence: 99%

The Effect of Chlorination on Organocyanide Compounds

Theis¹,

Young

2002

Water Environment Research

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Results are presented that explore the possibility of organocyanide compounds in wastewater contributing to elevated cyanide levels in the chlorinated effluents of publicly owned treatment works. Four model compounds, acetonitrile, amygdalin, cyanocobalamin, and 2-acetoxy-3-butenenitrile, were selected and tested with varying chlorine dosages for release of cyanide by total and diffusible cyanide procedures. The coenzyme form of vitamin B 12 , which does not contain cyanide, was also tested. It was found that acetonitrile and amygdalin do not yield cyanide with or without chlorination, cyanocobalamin had increased release with increased chlorine dosages, and 2-acetoxy-3butenenitrile had generally decreased release of cyanide with increased chlorine dosages. Both cyanocobalamin and coenzyme vitamin B 12 gave evidence of the formation of the cobalt-cyanide complex after chlorination, even though the molecular structure of the coenzyme vitamin B 12 contains no cyanide. Water Environ. Res., 74, 51 (2002).

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Introduction of the cyano group into the molecule

Cited by 56 publications

References 267 publications

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Synthesis of [¹⁴C] labeled 2‐methoxypyrimidine‐5‐carboxylic acid

The Effect of Chlorination on Organocyanide Compounds

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Introduction of the cyano group into the molecule

Cited by 56 publications

References 267 publications

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Changes in the Cellular Energy State Affect the Activity of the Bacterial Phosphotransferase System

Synthesis of [14C] labeled 2‐methoxypyrimidine‐5‐carboxylic acid

The Effect of Chlorination on Organocyanide Compounds

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Synthesis of [¹⁴C] labeled 2‐methoxypyrimidine‐5‐carboxylic acid