Structure, function and evolution of the Archaeal class I fructose-1,6-bisphosphate aldolase

Lorentzen, Esben; Siebers, Bettina; Hensel, Reinhard; Pohl, Ehmke

doi:10.1042/bst0320259

Cited by 33 publications

(30 citation statements)

References 23 publications

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“…The folding of the polypeptide chain of TBP aldolase, shown in supplemental Fig. S1, corresponds to a (␣/␤) 8 or triose-phosphate isomerase barrel fold that is typical of class I and II aldolases (44). The extensive conservation of the active site residues and their identical spatial disposition between class I FBP and TBP aldolases is consistent with the hypothesis of divergent evolution from a common ancestor (45).…”

Section: Discussionsupporting

confidence: 63%

Structure of a Class I Tagatose-1,6-bisphosphate Aldolase

LowKam

Liotard

Sygusch

2010

Journal of Biological Chemistry

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Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four diastereoisomers (fructose 1,6-bisphosphate (FBP), psicose 1,6-bisphosphate, sorbose 1,6-bisphosphate, and tagatose 1,6-bisphosphate) to dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate with high catalytic efficiency. To investigate its enzymatic mechanism, high resolution crystal structures were determined of both native enzyme and native enzyme in complex with dihydroxyacetone-P. The electron density map revealed a (␣/␤) 8 fold in each dimeric subunit. Flash-cooled crystals of native enzyme soaked with dihydroxyacetone phosphate trapped a covalent intermediate with carbanionic character at Lys 205 , different from the enamine mesomer bound in stereospecific class I FBP aldolase. Structural analysis indicates extensive active site conservation with respect to class I FBP aldolases, including conserved conformational responses to DHAP binding and conserved stereospecific proton transfer at the DHAP C3 carbon mediated by a proximal water molecule. Exchange reactions with tritiated water and tritium-labeled DHAP at C3 hydrogen were carried out in both solution and crystalline state to assess stereochemical control at C3. The kinetic studies show labeling at both pro-R and pro-S C3 positions of DHAP yet detritiation only at the C3 pro-S-labeled position. Detritiation of the C3 pro-R label was not detected and is consistent with preferential cis-trans isomerism about the C2-C3 bond in the carbanion as the mechanism responsible for C3 epimerization in tagatose-1,6-bisphosphate aldolase.Aldolases are crucial enzymes in living organisms because of their role in essential metabolic pathways, such as gluconeogenesis and glycolysis. Their ability to control the stereochemistry of the carbon-carbon bond formation makes them models for de novo preparation of carbohydrates (1) and ideal alternatives to traditional methods in synthetic organic chemistry (2-4). Tagatose-1,6-bisphosphate (TBP) 2 aldolase is an inducible enzyme that, although demonstrating greatest affinity for D-tagatose 1,6-bisphosphate, can also use as substrate the bisphosphorylated D-hexose stereoisomers: sorbose bisphosphate, psicose bisphosphate, and fructose bisphosphate (5). The four sugars are diastereoisomers and differ in stereochemistry at carbon 3 and at carbon 4 with respect to the configuration of their hydroxyl groups. The cleavage of the four sugars produces glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP), whereas the condensation of glyceraldehyde 3-phosphate and DHAP produces a mixture of the four D-hexoses in Staphylococcus aureus (5).Aldolases are broadly categorized with respect to their catalytic mechanism into two classes. Class I aldolases are characterized by formation of covalent Schiff base intermediates (6 -8), whereas class I...

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Section: Discussionsupporting

confidence: 63%

Structure of a Class I Tagatose-1,6-bisphosphate Aldolase

LowKam

Liotard

Sygusch

2010

Journal of Biological Chemistry

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“…kodakarensis (130,133). Despite the lack of significant overall sequence identity, the structural similarity of the two types of FBPA I enzymes suggests a common ancestry and, thus, homology (135,136). Together with the similar binding modes for Schiff base intermediates of the substrate DHAP, this strongly indicates a similar catalytic mechanism for the eukaryotic and the archaeal-type class I FBPAs.…”

Section: Fructose-16-bisphosphate Aldolase (Catabolic)mentioning

confidence: 70%

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

280

294

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SUMMARY The metabolism of Archaea , the third domain of life, resembles in its complexity those of Bacteria and lower Eukarya . However, this metabolic complexity in Archaea is accompanied by the absence of many “classical” pathways, particularly in central carbohydrate metabolism. Instead, Archaea are characterized by the presence of unique, modified variants of classical pathways such as the Embden-Meyerhof-Parnas (EMP) pathway and the Entner-Doudoroff (ED) pathway. The pentose phosphate pathway is only partly present (if at all), and pentose degradation also significantly differs from that known for bacterial model organisms. These modifications are accompanied by the invention of “new,” unusual enzymes which cause fundamental consequences for the underlying regulatory principles, and classical allosteric regulation sites well established in Bacteria and Eukarya are lost. The aim of this review is to present the current understanding of central carbohydrate metabolic pathways and their regulation in Archaea . In order to give an overview of their complexity, pathway modifications are discussed with respect to unusual archaeal biocatalysts, their structural and mechanistic characteristics, and their regulatory properties in comparison to their classic counterparts from Bacteria and Eukarya . Furthermore, an overview focusing on hexose metabolic, i.e., glycolytic as well as gluconeogenic, pathways identified in archaeal model organisms is given. Their energy gain is discussed, and new insights into different levels of regulation that have been observed so far, including the transcript and protein levels (e.g., gene regulation, known transcription regulators, and posttranslational modification via reversible protein phosphorylation), are presented.

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“…FBA, a very important enzyme for living organisms, is involved in sugar production and signaling. FBA has been studied in various species (especially in bacteria and vertebrates) with focus on its structure, kinetic parameter, and potential value in therapy and crop production (Giege et al, 2003;Lorentzen et al, 2004;Rodaki et al, 2006). However, there is no report on the FBA gene family in Arabidopsis.…”

Section: Discussionmentioning

confidence: 99%