Functional analysis of anomeric sugar kinases

Conway, Louis P.; Voglmeir, Josef

doi:10.1016/j.carres.2016.06.001

Cited by 16 publications

(10 citation statements)

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“…Phosphorylation of sugars provides two negative charges that prevent passive diffusion across the cell membrane, enabling intracellular concentration of intermediates [4]. Phosphorylation at both terminal hydroxyls permits reactions that split saccharides, such as the aldolase-catalyzed retro-aldol reactions in glycolysis [5]. Carbohydrate phosphorylation is sufficiently fundamental to cellular function that it is likely to have been developed early in evolution [6].…”

Section: Overview and Importancementioning

confidence: 99%

“…The reaction is performed by enzymes from five evolutionarily distinct classes (Table 1, Figure 1). These carbohydrate kinases transfer the terminal phosphate from a nucleoside triphosphate (usually ATP) to a free sugar hydroxyl [5]. Defects in carbohydrate phosphorylation have been associated with several diseases; in particular, autosomal galactokinase deficiencies lead to juvenile cataracts within weeks of birth [7,8], [17]).…”

Section: Overview and Importancementioning

confidence: 99%

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Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

2019

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Carbohydrate kinases activate a wide variety of monosaccharides by adding a phosphate group, usually from ATP. This modification is fundamental to saccharide utilization, and it is likely a very ancient reaction. Modern organisms contain carbohydrate kinases from at least five main protein families. These range from the highly specialized inositol kinases, to the ribokinases and galactokinases, which belong to families that phosphorylate a wide range of substrates. The carbohydrate kinases utilize a common strategy to drive the reaction between the sugar hydroxyl and the donor phosphate. Each sugar is held in position by a network of hydrogen bonds to the non-reactive hydroxyls (and other functional groups). The reactive hydroxyl is deprotonated, usually by an aspartic acid side chain acting as a catalytic base. The deprotonated hydroxyl then attacks the donor phosphate. The resulting pentacoordinate transition state is stabilized by an adjacent divalent cation, and sometimes by a positively charged protein side chain or the presence of an anion hole. Many carbohydrate kinases are allosterically regulated using a wide variety of strategies, due to their roles at critical control points in carbohydrate metabolism. The evolution of a similar mechanism in several folds highlights the elegance and simplicity of the catalytic scheme.

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Section: Overview and Importancementioning

confidence: 99%

Section: Overview and Importancementioning

confidence: 99%

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

2019

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“…The protein encoded by Traes_1BL_869ED1456 was corresponding to sugar kinase. As a super gene family, sugar kinases can be divided into many distinct nonhomologous families and they were involved in regulating many activities in plant cells such as energy metabolism and transport (Bork et al 1993;Conway and Josef 2016;Usuda et al 1997). The function of energy metabolism and transport is similar to Lr34/Yr18 or Lr67/Yr46.…”

Section: Discussionmentioning

confidence: 99%

Combining Single Nucleotide Polymorphism Genotyping Array with Bulked Segregant Analysis to Map a Gene Controlling Adult Plant Resistance to Stripe Rust in Wheat Line 03031-1-5 H62

Wang

et al. 2018

Phytopathology®

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Stripe rust, caused by Puccinia striiformis f. sp. tritici, is one of the most devastating diseases of wheat worldwide. Growing resistant cultivars is considered the best approach to manage this disease. In order to identify the resistance gene(s) in wheat line 03031-1-5 H62, which displayed high resistance to stripe rust at adult plant stage, a cross was made between 03031-1-5 H62 and susceptible cultivar Avocet S. The mapping population was tested with Chinese P. striiformis f. sp. tritici race CYR32 through artificial inoculation in a field in Yangling, Shaanxi Province and under natural infection in Tianshui, Gansu Province. The segregation ratios indicated that the resistance was conferred by a single dominant gene, temporarily designated as YrH62. A combination of bulked segregant analysis (BSA) with wheat 90K single nucleotide polymorphism (SNP) array was used to identify molecular markers linked to YrH62. A total of 376 polymorphic SNP loci identified from the BSA analysis were located on chromosome 1B, from which 35 kompetitive allele-specific PCR (KASP) markers selected together with 84 simple sequence repeat (SSR) markers on 1B were used to screen polymorphism and a chromosome region associated with rust resistance was identified. To saturate the chromosomal region covering the YrH62 locus, a 660K SNP array was used to identify more SNP markers. To develop tightly linked markers for marker-assisted selection of YrH62 in wheat breeding, 18 SNPs were converted into KASP markers. A final linkage map consisting of 15 KASP and 3 SSR markers was constructed with KASP markers AX-109352427 and AX-109862469 flanking the YrH62 locus in a 1.0 cM interval. YrH62 explained 63.8 and 69.3% of the phenotypic variation for disease severity and infection type, respectively. YrH62 was located near the centromeric region of chromosome 1BS based on the positions of the SSR markers in 1B deletion bins. Based on the origin, responses to P. striiformis f. sp. tritici races, and marker distances, YrH62 is likely different from the other reported stripe rust resistance genes/quantitative trait loci on 1B. The gene and tightly linked KASP markers will be useful for breeding wheat cultivars with resistance to stripe rust.

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“…This compound, being charged, has a reduced ability to traverse membranes and is thus trapped in the compartment where it was formed. Glc-6-P is an important intermediate of glycolysis (Conway and Voglmeir, 2016), but it can also be easily converted to Glc-1-P by phosphoglucomutase (PGM). Glc-1-P may also be produced by α-glucan phosphorylases from linear glucans (Stitt et al., 2010) or originate from fructose-6-phosphate (Fru-6-P), which is sequentially used by phosphoglucoisomerase (PGI) and PGM (Stitt et al., 2010) or by the breakdown of UDP-Glc via the reverse reaction of UGPases (Kleczkowski et al., 2010).…”

Section: Ugpase Enzymementioning

confidence: 99%

UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, Providing de novo Precursors for Glycosylation Reactions

Decker

Kleczkowski

2019

Front. Plant Sci.

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Nucleotide sugars are the key precursors for all glycosylation reactions and are required both for oligo- and polysaccharides synthesis and protein and lipid glycosylation. Among all nucleotide sugars, UDP-sugars are the most important precursors for biomass production in nature (e.g., synthesis of cellulose, hemicellulose, and pectins for cell wall production). Several recent studies have already suggested a potential role for UDP-Glc in plant growth and development, and UDP-Glc has also been suggested as a signaling molecule, in addition to its precursor function. In this review, we will cover primary mechanisms of formation of UDP-sugars, by focusing on UDP-sugar metabolizing pyrophosphorylases. The pyrophosphorylases can be divided into three families: UDP-Glc pyrophosphorylase (UGPase), UDP-sugar pyrophosphorylase (USPase), and UDP-N-acetyl glucosamine pyrophosphorylase (UAGPase), which can be distinguished both by their amino acid sequences and by differences in substrate specificity. Substrate specificities of these enzymes are discussed, along with structure-function relationships, based on their crystal structures and homology modeling. Earlier studies with transgenic plants have revealed that each of the pyrophosphorylases is essential for plant survival, and their loss or a decrease in activity results in reproductive impairment. This constitutes a problem when studying exact in vivo roles of the enzymes using classical reverse genetics approaches. Thus, strategies involving the use of specific inhibitors (reverse chemical genetics) are also discussed. Further characterization of the properties/roles of pyrophosphorylases should address fundamental questions dealing with mechanisms and control of carbohydrate synthesis and may allow to identify targets for manipulation of biomass production in plants.

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Functional analysis of anomeric sugar kinases

Cited by 16 publications

References 72 publications

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

Carbohydrate Kinases: A Conserved Mechanism Across Differing Folds

Combining Single Nucleotide Polymorphism Genotyping Array with Bulked Segregant Analysis to Map a Gene Controlling Adult Plant Resistance to Stripe Rust in Wheat Line 03031-1-5 H62

UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, Providing de novo Precursors for Glycosylation Reactions

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