Direct Oxygen Transfer in Enzymic Syntheses Coupled to Adenosine Triphosphate Degradation<sup>1</sup>

Boyer, Paul D.; Koeppe, Owen J.; Luchsinger, Wayne W.

doi:10.1021/ja01583a029

Cited by 87 publications

(19 citation statements)

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“…In a study with 18 O-labelled glutamate, it has been shown that I8 O appears in the phosphate produced, confirming the intennediate fonnation of glutamyl phosphate (8). This study indicated that the essential reaction takes place within a quaternary complex, a conclusion confirmed by the studies of Hartman & Buchanan (9) and Gass & Meiler (10).…”

Section: Introductionsupporting

confidence: 68%

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Doss

Tadros²

1991

Clinical Chemistry and Laboratory Medicine

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Section: Introductionsupporting

confidence: 68%

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Doss

Tadros²

1991

Clinical Chemistry and Laboratory Medicine

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“…The mechanism of the glutamine synthetase reaction has been studied with the aid of 018 in two laboratories (75,76). In both cases it was found that 018 in the carboxyl of glutamate is transferred to orthophosphate de rived from ATP and suffers no dilution from the oxygen of the medium.…”

Section: Glutaminementioning

confidence: 99%

Amino Acid and Protein Metabolism

Kamin¹,

Handler²

1957

Annu. Rev. Biochem.

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AMMONIAThe central metabolic position of ammonia has received renewed atten tion in recent years. To the list of known ammonia-producing reactions in mammals, summarized by Bessman (1), has been added the following: formylation of THF A2 from formiminoglutamate (2, 3) and, in microbial sources, L-alanine dehydrogenase (4); formylation from formimino glycine (S to 11); reductive deamination from glycine (12); and the degradation of glucosamine-6-phosphate (13). Since the fate of the nitrogen of numerous compounds is at present unknown, this list may be expected to expand an nually. Crystalline glutamic dehydrogenase isolated from corn leaves by Bulen (14) is DPN -specific, sensitive to sulfide reagents, and in general resembles the enzyme obtained from mammalian sources. Since the amino nitrogen of L-amino acids can be directed toward glutamate by transamina tion, it appears that glutamic dehydrogenase is the enzyme responsible for the major production of ammonia in hepatic metabolism in the steady state; it is not equally certain, however, that glutamic dehydrogenase universally occupies so central a role. Of various strains of B. subtilis which have been isolated, only those which possess glutamic dehydrogenase can use NH 3 as the sole nitrogen source (15). However, a mutant (5-) which can use am monia lacks glutamic dehydrogenase yet is capable of oxidizing glutamate (4). Fractionation of lysozyme-treated cells yielded a DPN-specific L-alanine 1 The survey of the literature pertaining to this review included journals received through Novemb er, 1956.2 The following abbreviations are used in this chapter: AICAR for 4-amino 5-imidazole carboxamide ribotide; ADP for adenosinediphosphate; AMP for adeno sinemonophosphate; ATP for adenosinetriphosphate; CoA for coenzyme Aj CSA for cysteine sulfinic acid; CTP for cytidinetriphosphate; DAP for diaminopimelic acid; DNA for deoxyribonuc leic acid; DNP for 2,4-dinitrophenol; DOPA for 3,4-dihydroxy phenylalanine; DPN for diphosphopyridine nucleotide; DPNH for diphosphopyridine nucleotide (reduced form); EDT A for ethylenediamine tetraacetic acid ; FAD for flavin adenine dinucleotide; FI G for formimino glycine; FGAR for formyl glycinamide ribotide; FMN for riboflavin phosphate; GAR for glycinamide ribotide; GDP for guanosinediphosphate; GMP for guanosinemonophosphate; GTP for guanosinetri phosphate; IDP for inosine diphosphate; IGP for imidazole glycerol phosphate; IMP for inosinemonophosphate; INH for isonicotinylhydrazide; ITP for inosinetriphos phate; PCMB for p-chloromercuribenzoate; Pi for inorganic phosphate; PBi for in organic pyrophosphate; PRPP for 5-phosphoribosylpyrophosphate; RNA for ribo nucleic acid; THF A for tetrahydrofolic acid; TPN for triphosphopyridine nucleotide; TPNH fortriphosphopyridine nucleotide (reduced form); Tris for trishydroxymethyl aminomethane; and UTP for uridinetriphosphate. 419Annu. Rev. Biochem. 1957.26:419-490. Downloaded from www.annualreviews.org Access provided by Texas Christian University on 02/03/15. For personal use only.Quick l...

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“…This phosphotransfer reaction shows a close analogy to the mechanism postu lated for the glutamine synthetase reaction (59,60); "active glycine" may play a role in the biosynthesis of gIycinamide ribotide.…”

Section: Definition and Nomenclaturementioning

confidence: 68%

Transferases

Hoffmann-Ostenhof¹

1960

Annu. Rev. Biochem.

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Until now the subject of transferases has never been treated in an in dependent article in the Annual Review oj Biochemistry. These enzymes have hitherto been dealt with in various chapters, mostly under "Nonoxidative, Nonproteolytic Enzymes." The rapidly increasing number of transferases, as well as the great importance of these enzymes in almost all major metabolic processes, may justify an independent treatment of transferases in these 1 The survey of the literature pertaining to this review was completed in Septem_ ber, 1959. 2 The following abbreviations,are used: AMP for adenosine monophosphate; CDP for cytidine diphosphate; CMP for cytidine monophosphate; CTP for cytidine tri phosphate; CoA for coenzyme A; G DP for guanosine diphosphate; GMP for guanosine monophosphate; GTP for guanosine triphosphate; IDP for inosine diphosphate; IMP for inosine monophosphate; ITP for inosine triphosphate; Pi for ' orthophos phate; PP for pyrophosphate ; THFA for tetrahydrofolic acid; UDP for uridine di phosphate; UMP for uridine monophosphate; UTP for uridine triphosphate. 73 Annu. Rev. Biochem. 1960.29:73-104. Downloaded from www.annualreviews.org Access provided by Yale University -Law Library on 02/03/15. For personal use only. Quick links to online content Further ANNUAL REVIEWS HOFFMANN-OSTENHOFbooks and treatises on enzymes. Accordingly, papers on hydrolyzing enzymes will not be considered here, even if these enzymes show, in addition to their hydrolytic action, a real transfer actio � according to the definition given above. Nomenclature of enzymes in general is, at present, in a process of revision. The Enzyme Commission, which was established a few years ago within the framework of the International Union of Biochemistry, intends to devise rules for a rational nomenclature of all enzymes, the main use of which will be for indexing and abstracting purposes. In addition, recommendations for trivial names will be made, as the rational names are often too unwieldy. Although the work of the Commission has n � t yet been finished, the rules for the rational naming of transferases seem to be quite final and, in part, have already been made public (3). According to these rules, a transferase should be named rationally following the scheme: group donor-group ac ceptor-group transferred-transferase. Thus, the well-known enzyme cata lyzing the reversible transfer of an amino group from L-alanine to a-keto glutaric acid should rationally be named L-alanine a-ketoglutarate amino transferase. In regard to the direction to be chosen for enzymes catalyzing reversible reactions, it is suggested that, in all cases where ATP is involved in a transfer reaction, this compound should always be named as the donor, whereas a-ketoglutarate should always be named as the acceptor in amino group transfer. In reactions for which these rules cannot be applied, the sub strate with higher mol. wt. should be named as the donor. The latter rule can not, however, be considered final.According to these rules, all enzymes catalyzing simple transfer ...

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Direct Oxygen Transfer in Enzymic Syntheses Coupled to Adenosine Triphosphate Degradation¹

Cited by 87 publications

References 1 publication

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Amino Acid and Protein Metabolism

Transferases

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Direct Oxygen Transfer in Enzymic Syntheses Coupled to Adenosine Triphosphate Degradation1

Cited by 87 publications

References 1 publication

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Effect of Ascaris lumbricoides Infection on Brain Enzymes

Amino Acid and Protein Metabolism

Transferases

Contact Info

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Resources

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Direct Oxygen Transfer in Enzymic Syntheses Coupled to Adenosine Triphosphate Degradation¹