The enzymic synthesis of aryl sulphamates

Ab, Roy

doi:10.1016/0006-3002(58)90262-2

Cited by 23 publications

(5 citation statements)

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“…The pH optimum here was lower than with phenol as acceptor, but this may concern the state of ionization of the reactants rather than the partici pation of different enzymes. (87,88) has studied preparations from rat or guinea pig liver, using 2-naphthylamine or aniline as acceptors. The sulfate donor was shown to be PAPS, but the arylamine sulfokinase was apparently different from phenol sulfokinase [Gregory & Lipmann (42)] in that it required Mg++ for maximal activity; it, too, is inhibited by sulfhydryl-blocking reagents.…”

Section: Sulfokinasesmentioning

confidence: 99%

Metabolism of Sulfur Compounds (Sulfate Metabolism)

Gregory¹,

Robbins²

1960

Annu. Rev. Biochem.

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SO much work has been published on sulfur compounds in the fourteen years since the last review in this series [Lugg (1)] that we have not attempted to cover the whole field. This paper is regretfully restricted to the metabo lism of sulfate, and many other areas must be slighted in which valuable developments have appeared. However, a few outstanding reviews and general works dealing with particular sulfur compounds should be mentioned: methionine (2), glutathione (3), lipoic acid (4), biotin and other compounds (5), protein sulfhydryl groups (6, 7), and a collection of papers in memory of C. Fromageot, including his complete bibliography (8). General reviews on sulfur metabolism have been published by Bersin (9), Young & Maw (10), and Dziewiatkowski (11).Although many good whole animal studies have appeared on the in corporation and distribution of sulfate [Dziewiatkowski (12)] and on the conjugation of phenolic compounds with sulfate, we shall report mainly en zymological work. Recent knowledge of enzyme reactions involving sulfate has been reviewed by Lipmann (13). The activation of sulfate to form a "high -energy" intermediate is the first step in its assimilation. Two paths are then open: the sulfate may be reduced, or it may be transferred. in which case the reaction is catalyzed by sulfokinases and various esters are formed. And finally, there are hydrolytic enzymes, the sulfatases, which split almost all sulfate esters. SULFATE ACTIVATIONDeMeio and his co-workers were the first to study phenyl sulfate forma tion in a ho mogenate (14). They showed that in a liver homogenate oxygen and mitochondria were necessary for phenyl sulfate synthesis and that ATP would replace these requirements (15). These workers were also among the first to show that the sulfate activating and -transferring systems could be separated (16). Bernstein & McGilvery (17) studied the conjugation of m aminophcnol in liver homogenatcs. By studying the kinetics of this system, they deduced that an intermediate activated sulfate was formed and that at least two enzymes were involved (18). They also showed that a com pound accumulated that would rapidly transfer sulfate when ATP, sulfate, 1 The survey of the literature pertaining to this review was concluded in September 1959.2 The following abbreviations are used in this review: AMP for adenosine mono phosphate; APS for adenosine-5'-phosphosulfate; p-NP and p-NPS for p-nitrophenol and its sulfate, respectively; PAP for 3'-phosphoadenosine-5 '-phosphate; PAPS for 3'-phosphoadenosine-5'-phosphosuJfate; PP for pyrophosphate; TPN+ and TPNH for oxidized and reduced tripho5phopyridine nucle otide, respectively. 347Annu. Rev. Biochem. 1960.29:347-364. Downloaded from www.annualreviews.org Access provided by Western Michigan University on 02/02/15. For personal use only.Quick links to online content Further ANNUAL REVIEWS

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Section: Sulfokinasesmentioning

confidence: 99%

Metabolism of Sulfur Compounds (Sulfate Metabolism)

Gregory¹,

Robbins²

1960

Annu. Rev. Biochem.

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“…Most STs that sulfate hydroxy groups and only a few STs that sulfate amino groups have been reported (i.e. in arylamine ST [Roy 1960, Hernández et al 1991 and N-heparan sulfate ST [Hashimoto et al 1992]). Compounds described as substrates for these STs were not effective for N-ST activity in the standard condition.…”

Section: Resultsmentioning

confidence: 99%

“…STs from intestinal bacteria are magnesium-dependent enzymes, which are activated by Mg 2ϩ and Co 2ϩ , Lee et al 1995. Arylamine ST was reported to require Mg 2ϩ for optimal activity (Roy 1960). However, most STs do not require cations for enzyme activity.…”

Section: Resultsmentioning

confidence: 99%

PURIFICATION AND CHARACTERIZATION OF A SULFOTRANSFERASE SPECIFIC TO N‐21 OF SAXITOXIN AND GONYAUTOXIN 2+3 FROM THE TOXIC DINOFLAGELLATE GYMNODINIUM CATENATUM (DINOPHYCEAE)

Sako

Yoshida

Uchida

et al. 2001

Journal of Phycology

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A sulfotransferase (ST) specific to N‐21 of saxitoxin (STX) and gonyautoxin 2+3 (GTX2+3) designated as N‐ST was purified to homogeneity from the cytosolic fraction of clonal‐axenic vegetative cells of the toxic dinoflagellate Gymnodinium catenatum Graham GC21V, which causes paralytic shellfish poisoning. The enzyme transferred a sulfate group from 3′‐phosphoadenosine 5′‐phosphosulfate (PAPS) to N‐21 in the carbamoyl group of STX and GTX2+3 to produce GTX5 and C1+2, respectively. The molecular mass of the purified enzyme was determined by SDS‐PAGE to be 59 kDa. Gel filtration chromatography showed a native molecular mass of 65 kDa, indicating that the N‐ST is a monomeric enzyme. The N‐ST was specific to only N‐21 of STX and GTX2+3, and O‐22 sulfation was not observed. Moreover, the N‐ST was not active toward neo STX and GTX1+4, which differed from STX and GTX2+3, respectively, in only N‐1 hydroxylation. When various compounds previously reported to be substrates for STs in other organisms and paralytic shellfish poisoning toxins other than STX and GTX2+3 were added to the reaction mixture, N‐ST activity was not decreased. The enzyme required PAPS as the sole source of sulfate. The enzyme was optimally active at pH 6.0 and 25° C, and its activity was enhanced by Mg2+ and Co2+. The Km values of the N‐ST for STX and GTX2+3 were 16.1 μM and 29.8 μM, respectively.

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“…Little affinity at acid pH (K = 0-36M at pH 5-5); greater stability (K = 0.03M) at pH 7. It has recently been demonstrated that enzyme preparations from mammalian liver (Roy, 1958) and sheep intestinal mucosa (Kent & Pasternak, 1958) can synthesize aryl sulphamates from certain arylamines in the presence of S042ions and ATP. The present communication describes results obtained in a study of this synthesis using quantitative methods.…”

Section: On the Intramolecular Location Of Deoxyribonucleotides Incorporated Into Deoxyribonucleicmentioning

confidence: 99%

“…The present communication describes results obtained in a study of this synthesis using quantitative methods. The enzyme preparations were obtained from liver by methods previously described (Roy, 1956).…”

Section: On the Intramolecular Location Of Deoxyribonucleotides Incorporated Into Deoxyribonucleicmentioning

confidence: 99%

Proceedings of the Biochemical Society

1959

Biochemical Journal

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The fluorescence of solutions of phenol, cresol and indole in propylene glycol at -70°in layers of 20-30 iL thickness showed concentration depolarization (Forster, 1951; Weber, 1954) over the range 0-01-0-1 M. The characteristic distances B for which the chances of transfer and emission are equal is for both phenol and indole 171. Transfer in indole is only observed when the wavelength of excitation is shorter than 300 m,. Even 04m-indole solutions show strong polarization when excited with 310m,u light. In mixtures of phenol and indole studied under the same conditions polarization and fluorescence spectral measurements show transfer from phenol to indole with R = 20A. Proteins that do not contain tryptophan (zein, insulin, ribonuclease), dissolved in 50 % propylene glycolwater mixtures at -70°and excited with light of 275-290 m, wavelength show polarizations of b

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The enzymic synthesis of aryl sulphamates

Cited by 23 publications

References 4 publications

Metabolism of Sulfur Compounds (Sulfate Metabolism)

Metabolism of Sulfur Compounds (Sulfate Metabolism)

PURIFICATION AND CHARACTERIZATION OF A SULFOTRANSFERASE SPECIFIC TO N‐21 OF SAXITOXIN AND GONYAUTOXIN 2+3 FROM THE TOXIC DINOFLAGELLATE GYMNODINIUM CATENATUM (DINOPHYCEAE)

Proceedings of the Biochemical Society

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