Adenylate Kinase from Bakers' Yeast

Su, Shirley; Russell, Percy J.

doi:10.1016/s0021-9258(18)92018-1

Cited by 35 publications

(5 citation statements)

References 16 publications

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“…Proposed Reaction Mechanism of the NTP-AMP Transphosphorylase. The reaction mechanism of adenylate kinase and NTP-NDP kinase are well known (Callaghan and Weber, 1955;Markland and Wadkins, 1966;Mourad and Parks, 1966;Glaze and Wadkins, 1967;Goffeau et al, 1967;Su and Russell, 1968). From the results described in this paper conclusions could be drawn for the reaction mechanism of the NTP-AMP transphosphorylase.…”

Section: Discussionmentioning

confidence: 53%

Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria

Gj¹

1970

Biochemistry

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Section: Discussionmentioning

confidence: 53%

Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria

Gj¹

1970

Biochemistry

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“…It has also been observed that binding of AMP can cause enhancement of fluorescence for probes bound to the ATP site, supporting the model where AMP causes conformational changes in the ATP site upon binding to the AMP site (Chaun et al, 1989). Kinetic studies of adenylate kinase from various sources reveal a rapid equilibrium random sequential mechanism for adenylate kinase (Rhoads & Lowenstein, 1968;Su & Russel, 1968;Markland & Wadkins, 1966;Font & Gautheron, 1980;Huss et al, 1989). In enzymes having this mechanism, both substrates bind randomly to the enzyme.…”

Section: Discussionmentioning

confidence: 80%

Substrate Binding Causes Movement in the ATP Binding Domain of Escherichia coli Adenylate Kinase

et al. 1996

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Crystallographic evidence suggests that there is a large hinged domain motion associated with substrate binding in adenylate kinase. To test this hypothesis, resonance energy transfer measurements of substrate binding were initiated. Adenylate kinase from Escherichia coli consists of three domains: the main body of the enzyme with alpha-helical and beta-sheet secondary structure, and domains that close over the AMP and ATP binding sites. Four single tryptophan mutants were constructed to map distances. Two tryptophan mutants were positioned at residues 133 (Y133W) and 137 (F137W), which are in the domain that closes over the ATP binding site. Mutant F86W that is located at the AMP binding site, and mutant S41W that is in the loop that close over AMP, complete the mapping library. Energy transfer was measured between each of these tryptophans and 5-[[2-(acetylamino)ethyl]amino]naphthalene-1-sulfonic acid (AEDANS) covalently bound to the single cysteine residue at position 77, which is located in the main body of adenylate kinase. The distance between the tryptophan of the F137W mutant adenylate kinase and the AEDANS-labeled Cys-77 decreased by 12.1 A upon the binding of the bisubstrate inhibitor P1, P5-bis(5'-adenosyl) pentaphosphate (AP5A). There were only small alterations in the tryptophan to Cys-77-AEDANS distances in the Y133W, F86W, and S41W mutants upon the binding of AP5A, ATP, or AMP, implying that movement of residues 133, 86, and 41 in relation to the Cys-77 residue was minimal. These results suggest that there is significant closure of the ATP binding domain upon the binding of ATP or AP5A. Unexpectedly, exposure of the enzyme to AMP also introduced a partial closure of the ATP hinged domain.

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“…Km values for ADP of the E. coli adenylate kinase have been obtained previously by treating the kinetic data under the assumption that the two binding sites of ADP on the enzyme are identical (Su & Russell, 1968;Ito et al, 1980;Saint Girons et al, 1987;Reinstein et al, 1989). This treatment may produce misleading results since AK has two binding sites for adenine nucleotides with different affinities and specificities and also different specificities for the same ligand, depending on whether or not it is complexed to Mg2+.…”

Section: Resultsmentioning

confidence: 99%

“…The mammalian cytosolic forms of pig and rabbit adenylate kinases (AK1) obey a random bi-bi rapid equilibrium kinetic mechanism, where the rate-limiting steps in catalysis were assigned to interconversion of the ternary complex between protein and substrates (Su & Russell, 1968) or to the dissociation of products (Rhoads & Lowenstein, 1968) from the protein. The stereochemical course of the catalyzed reaction was shown to follow an SN2 mechanism, which suggests a direct transfer of the phosphoryl group without covalent enzymatic intermediates (Richard & Frey, 1978).…”

mentioning

confidence: 99%

Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases

Reinstein¹,

Vetter²,

Schlichting³

et al. 1990

Biochemistry

107

112

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A new system for measurement of affinities of adenylate kinases (AK) for substrates and inhibitors is presented. This system is based on the use of the fluorescent ligand alpha,omega-di[(3' or 2')-O-(N-methylanthraniloyl)adenosine-5'] pentaphosphate (mAP5Am), which is an analogue of the bisubstrate inhibitor diadenosine pentaphosphate (AP5A). It allows the determination of dissociation constants for any ligand in the range of 1 x 10(-9) to 5 x 10(-2) M. Affinities for different bisubstrate inhibitors (AP4A, AP5A, AP6A) and substrates (AMP, ADP, ATP, GTP) were determined in the presence and absence of magnesium. An analysis of the binding of bisubstrate inhibitors is proposed and applied to these data. The techniques are used to describe the properties of a mutant enzyme with Gln-28----His (Q28H) prepared by site-directed mutagenesis in comparison to those of wild-type AK from Escherichia coli. This newly introduced histidine is already present in most other adenylate kinases and was regarded to be important or even essential for the catalytic reaction of AK. Temperature denaturation experiments indicate that the mutant enzyme has the same thermal stability as the wild-type enzyme and, as NMR studies indicate, also a very similar structure. However, steady-state catalytic studies and binding experiments showed that the affinities for substrates and inhibitors are elevated from 3-fold (AMP) to 5-fold (ATP) to 15-fold (AP5A) compared to those of the wild-type enzyme. Together with the results obtained by Tian et al. [Tian, G., Sanders, C. R., Kishi, F., Nakazawa, A., & Tsai, M.-D. (1988) Biochemistry 27, 5544-5552] on the effect of replacement of the conserved His-36 in the cytosolic AK (AK1) from chicken by glutamine and asparagine, this shows that residues 28 of AK from E. coli (AKec) and 36 of AK1 are situated in a comparable environment and are not essential for catalytic activity.

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Adenylate Kinase from Bakers' Yeast

Cited by 35 publications

References 16 publications

Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria

Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria

Substrate Binding Causes Movement in the ATP Binding Domain of Escherichia coli Adenylate Kinase

Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases

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