Glucose‐6‐Phosphate Dehydrogenases

Hr, Levy

doi:10.1002/9780470122938.ch3

Cited by 103 publications

(34 citation statements)

References 363 publications

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“…The archetypal subfamily of this group is the β-PGMs proper, which catalyze the inter-conversion of β-Dglucose 1-phosphate and D-glucose 6-phosphate. 128 This family contains a conserved histidine and GxxR motif in the cap, which are critical for substrate recognition by contacting the phosphate and sugar moieties, respectively. 129 In the related CbbY subfamily (typified by Rhodobacter CbbY; 130 Table 1), the histidine is likewise universally conserved, but the arginine is present only in a subset of proteins.…”

Section: Simple Bi-helical Cap Familiesmentioning

confidence: 99%

Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

Burroughs¹,

Allen²,

Dunaway‐Mariano³

et al. 2006

Journal of Molecular Biology

386

520

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The HAD (haloacid dehalogenase) superfamily includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates. The availability of numerous crystal structures of representatives belonging to diverse branches of the HAD superfamily provides us with a unique opportunity to reconstruct their evolutionary history and uncover the principal determinants that led to their diversification of structure and function. To this end we present a comprehensive analysis of the HAD superfamily that identifies their unique structural features and provides a detailed classification of the entire superfamily. We show that at the highest level the HAD superfamily is unified with several other superfamilies, namely the DHH, receiver (CheY-like), von Willebrand A, TOPRIM, classical histone deacetylases and PIN/FLAP nuclease domains, all of which contain a specific form of the Rossmannoid fold. These Rossmannoid folds are distinguished from others by the presence of equivalently placed acidic catalytic residues, including one at the end of the first core β-strand of the central sheet. The HAD domain is distinguished from these related Rossmannoid folds by two key structural signatures, a "squiggle" (a single helical turn) and a "flap" (a beta hairpin motif) located immediately downstream of the first β-strand of their core Rossmanoid fold. The squiggle and the flap motifs are predicted to provide the necessary mobility to these enzymes for them to alternate between the "open" and "closed" conformations. In addition, most members of the HAD superfamily contains inserts, termed caps, occurring at either of two positions in the core Rossmannoid fold. We show that the cap modules have been independently inserted into these two stereotypic positions on multiple occasions in evolution and display extensive evolutionary diversification independent of the core catalytic domain. The first group of caps, the C1 caps, is directly inserted into the flap motif and regulates access of reactants to the active site. The second group, the C2 caps, forms a roof over the active site, and access to their internal cavities might be in part regulated by the movement of the flap. The diversification of the cap module was a major factor in the exploration of a vast substrate space in the course of the evolution of this superfamily. We show that the HAD superfamily contains 33 major families distributed across the three superkingdoms of life. Analysis of the phyletic patterns suggests that at least five distinct HAD proteins are traceable to the last universal common ancestor (LUCA) of all extant organisms. While these prototypes diverged prior to the emergence Abbreviations used: HAD, haloacid dehalogenase; PNKP, polynucleotide kinase phosphatase; KDO 8-P, deoxy-Dmannose-octulosonate 8-phosphate; CTD, carboxyl-terminal domain; PNKP, polynucleotide kinase phosphatase; LUCA, last universal common ancestor.E-mail address of the corresponding author: aravind@ncbi.nlm.nih.gov of the LUCA, t...

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Section: Simple Bi-helical Cap Familiesmentioning

confidence: 99%

Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

Burroughs¹,

Allen²,

Dunaway‐Mariano³

et al. 2006

Journal of Molecular Biology

386

520

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“…It was characterised in 1962 by Kirkman and Henderickson in human erythrocytes [4]. By 1979, G6PD was isolated and characterised in red blood cells and yeast cells [3]. Ever since then it has been identified in various organisms ranging from prokaryotes to humans, including bacteria, algae, fungi and ferns.…”

Section: Historical Background and Distribution Of Glucose 6-phosphate mentioning

confidence: 99%

“…The Nterminal was identified to be pyroglutamic acid, while that from Saccharomyces cerevisiae was tyrosine [83,84]. The N-terminals from the two subunits of C. utilus are glycine and alanine [3]. The C-terminals of the two C. utilus subunits are the same though; they consist of glycine [80].…”

Section: Primary Structure Of G6pdmentioning

confidence: 99%

“…1.1.1.49) belongs to the oxidoreductase classes of enzymes and are peculiar to Pentose Phosphate Pathway (also called the Hexose Monophosphate Shunt or the phosphogluconate pathway) [2,3]. The Pentose Phosphate Pathway (PPP) is involved in the generation of reducing power, NADPH (reduced nicotinamide adenine dinucleotide phosphate), common to non-photosynthetic cells and organisms [2,3]. This pathway is also involved in the synthesis of ribose 5-phosphate which is highly essential for diving cells to produce RNA, DNA and coenzymes such as ATP, NADH and coenzyme A [2,3].…”

Section: Introductionmentioning

confidence: 99%

“…The Pentose Phosphate Pathway (PPP) is involved in the generation of reducing power, NADPH (reduced nicotinamide adenine dinucleotide phosphate), common to non-photosynthetic cells and organisms [2,3]. This pathway is also involved in the synthesis of ribose 5-phosphate which is highly essential for diving cells to produce RNA, DNA and coenzymes such as ATP, NADH and coenzyme A [2,3].…”

Section: Introductionmentioning

confidence: 99%

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Updates on Glucose 6-Phosphate Dehydrogenase (G6PD): From Prokaryotes to Human

2016

IJSR

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Glucose 6-phosphate dehydrogenase (G6PD) is the rate determining enzyme that catalyzes the first step in pentose phosphate pathway (PPP) which produces NADPH that serves as reducing agent for reductive biosynthetic reactions such as steroids, fatty acids and nucleotides syntheses. Been ubiquitous, it has been found in wide range of organisms, ranging from prokaryotic organisms to even higher animals like human. Numerous G6PD isoenzymes have been isolated, purified and well characterised. However, obtained information such as its kinetic parameters and biological properties have not been judiciously appropriated for biotechnological/medical applications. This review thus concisely showcases G6PD, focusing on some sources where it has been isolated, purified and characterized, physicochemical/biochemical properties, the benefits and adverse effects its evolution may confer, and the possible biotechnological applications/prospects for the enzyme.

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