The Amidotransferases

Buchanan, John M.

doi:10.1002/9780470122846.ch2

Cited by 48 publications

(20 citation statements)

References 214 publications

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“…The amidotransferases were initially reviewed in this series in 1973 (Buchanan, 1973). The emphasis of this paper was on enzymology and biochemical characterization.…”

Section: Introductionmentioning

confidence: 99%

Enzymes Utilizing Glutamine as an Amide Donor

Zalkin

Smith

1998

Advances in Enzymology - And Related Areas of Molecular Biology

163

173

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“…The amidotransferases were initially reviewed in this series in 1973 (Buchanan, 1973). The emphasis of this paper was on enzymology and biochemical characterization.…”

Section: Introductionmentioning

confidence: 99%

Enzymes Utilizing Glutamine as an Amide Donor

Zalkin

Smith

1998

Advances in Enzymology - And Related Areas of Molecular Biology

163

173

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“…The finding that domains related to the five SCOP superfamilies are in fact members of one fold‐based superfamily leads to new insight into the evolution of enzymes in the de novo purine biosynthesis. Purine is synthesized in microorganisms by a pathway involving 10 successive enzymes (Buchanan 1973): PurF, PurD, PurT, PurL, PurM, PurK, PurE, PurC, PurB, and PurH, in which the six underlined enzymes use ATP as a substrate. The three‐dimensional structures have been determined for all of these ATP‐using enzymes, except PurL.…”

Section: Resultsmentioning

confidence: 99%

Finding evolutionary relations beyond superfamilies: Fold‐based superfamilies

et al. 2003

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Superfamily classifications are based variably on similarity of sequences, global folds, local structures, or functions. We have examined the possibility of defining superfamilies purely from the viewpoint of the global fold/function relationship. For this purpose, we first classified protein domains according to the ␤-sheet topology. We then introduced the concept of kinship relations among the classified ␤-sheet topology by assuming that the major elementary event leading to creation of a new ␤-sheet topology is either an addition or deletion of one ␤-strand at the edge of an existing ␤-sheet during the molecular evolution. Based on this kinship relation, a network of protein domains was constructed so that the distance between a pair of domains represents the number of evolutionary events that lead one from the other domain. We then mapped on it all known domains with a specific core chemical function (here taken, as an example, that involving ATP or its analogs). Careful analyses revealed that the domains are found distributed on the network as >20 mutually disjointed clusters. The proteins in each cluster are defined to form a fold-based superfamily. The results indicate that >20 ATP-binding protein superfamilies have been invented independently in the process of molecular evolution, and the conservative evolutionary diffusion of global folds and functions is the origin of the relationship between them.

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“…These enzymes catalyze the transfer of the amide group of L-glutamine, the source of nitrogen for most biosynthetic pathways, to an acceptor substrate, which is different for each glutaminedependent amidotransferase, to produce one molecule of L-glutamate and one molecule of aminated (or amidated) product. To date 13 different glutamine-dependent amidotransferases have been identified [16][17][18][19]. The enzymes are involved in the biosynthesis of nucleotides, amino acids, aminated sugars and antibiotics.…”

Section: Biochemistry Of Glutamate Synthasementioning

confidence: 99%

Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate

Heuvel

Curti

Vanoni

et al. 2004

Cellular and Molecular Life Sciences (CMLS)

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Glutamate synthase is a multicomponent iron-sulfur flavoprotein belonging to the class of N-terminal nucleophile amidotransferases. It catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. In recent years the X-ray structures of the ferredoxin-dependent glutamate synthase and of the a subunit of the NADPH-dependent glutamate synthase have become available. Thanks to X-ray crystallography, it is now known that the ammonia reaction intermediate is transferred via an intramolecular tunnel from the amidotransferase domain to the synthase domain over a distance of about 32A. Although ammonia channeling is a recurrent theme for N-terminal nucleophile and triad-type amidotransferases, the molecular mechanisms of ammonia transfer and its control are different for each known amidotransferase. This review focuses on the intriguing mechanism of action and self-regulation of glutamate synthase with a special focus on the structural data.

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The Amidotransferases

Cited by 48 publications

References 214 publications

Enzymes Utilizing Glutamine as an Amide Donor

Enzymes Utilizing Glutamine as an Amide Donor

Finding evolutionary relations beyond superfamilies: Fold‐based superfamilies

Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate

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