Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps

Cordeiro, Artur T.; Godoi, Paulo H.; Silva, Carlos Henrique Tomich de Paula da; Garratt, R.C.; Oliva, Glaucius; Thiemann, Otávio Henrique

doi:10.1016/s1570-9639(02)00464-8

Cited by 30 publications

(30 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PGI structures have been solved from a variety of mammalian sources and from B. stearothermophilus in native, inhibitor, and substrate (F6P)-bound forms (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25). CD spectra analysis and secondary structure predictions suggest a similar fold of the PGI/PMI from A. pernix and T. acidophilum and e.g.…”

Section: Molecular and Thermophilic Properties-thementioning

confidence: 99%

Bifunctional Phosphoglucose/Phosphomannose Isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum Constitute a Novel Enzyme Family within the Phosphoglucose Isomerase Superfamily

Hansen

Wendorff

Schönheit

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

The hyperthermophilic crenarchaeon Aeropyrum pernix contains phosphoglucose isomerase (PGI) activity. However, obvious homologs with significant identity to known PGIs could not be identified in the sequenced genome of this organism. The PGI activity from A. pernix was purified and characterized. Kinetic analysis revealed that, unlike all known PGIs, the enzyme catalyzed reversible isomerization not only of glucose 6-phosphate but also of epimeric mannose 6-phosphate at similar catalytic efficiency, thus defining the protein as bifunctional phosphoglucose/phosphomannose isomerase (PGI/PMI). The gene pgi/pmi encoding PGI/PMI (open reading frame APE0768) was identified by matrixassisted laser desorption ionization time-of-flight analyses; the gene was overexpressed in Escherichia coli as functional PGI/PMI. Putative PGI/PMI homologs were identified in several (hyper)thermophilic archaea and two bacteria. The homolog from Thermoplasma acidophilum (Ta1419) was overexpressed in E. coli, and the recombinant enzyme was characterized as bifunctional PGI/PMI. PGI/PMIs showed low sequence identity to the PGI superfamily and formed a distinct phylogenetic cluster. However, secondary structure predictions and the presence of several conserved amino acids potentially involved in catalysis indicate some structural and functional similarity to the PGI superfamily. Thus, we propose that bifunctional PGI/PMI constitutes a novel protein family within the PGI superfamily.Phosphoglucose isomerase (PGI 1 ; EC 5.3.1.9) catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. PGI plays a central role in sugar metabolism of eukarya, bacteria, and Archaea both in glycolysis via the Embden-Meyerhof pathway in eukarya and bacteria and in its modified versions found in Archaea. PGI is also involved in gluconeogenesis where the enzyme operates in the reverse direction (for the literature see Refs. 1-3). PGIs from the domains of eukarya and bacteria are well studied enzymes. A variety of PGIs have been purified and biochemically characterized, and the encoding genes have been cloned and sequenced (e.g. Refs. 4 -11). Crystal structures have been determined for the eukaryotic PGIs from pig, rabbit, human, and from the bacterium Bacillus stearothermophilus, and conserved amino acids proposed to be involved in substrate binding and/or catalysis have been identified (12-15, 17, 18, 20 -25). The eukaryal and bacterial PGIs belong to the PGI superfamily defined by its two conserved signature patternsTo date this superfamily includes more than 300 PGI sequences (see www.sanger.ac.uk/cgi-bin/Pfam/getacc?PF00342) (26) from bacteria and eukarya but only three from the archaeal domain. These include the PGI from the hyperthermophilic euryarchaeon Methanococcus jannaschii (MjPGI). This PGI has recently been characterized as the first archaeal member of the PGI superfamily. 2 So far little is known about other archaeal PGIs. Recently, two other euryarchaeal PGIs have been characterized, one from the hyperthermophilic euryarch...

show abstract

Section: Molecular and Thermophilic Properties-thementioning

confidence: 99%

Bifunctional Phosphoglucose/Phosphomannose Isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum Constitute a Novel Enzyme Family within the Phosphoglucose Isomerase Superfamily

Hansen

Wendorff

Schönheit

2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…It is known that C‐terminal domains are crucial to the sugar ring‐opening step catalysed by this enzyme. As the isomerization activity occurs at the dimer interface, the dimer structure of this enzyme is critical to its catalytic function . In addition, this variant was not found in either the Exome Aggregation Consortium or 1000 Genomes databases and all predictive software used classified it as deleterious.…”

Section: Discussionmentioning

confidence: 99%

Detection of new pathogenic mutations in patients with congenital haemolytic anaemia using next‐generation sequencing

Barreto

Arrizabalaga

Hoz

et al. 2016

Int J Lab Hematology

View full text Add to dashboard Cite

Summary Introduction Congenital haemolytic anaemia (CHA) refers to a group of genetically heterogeneous disorders, mainly caused by changes in genes encoding globin chains, cytoskeletal proteins and red cell enzymes, in which accurate diagnosis can be challenging with conventional techniques. Methods To set‐up a comprehensive assay for detecting mutations that could improve aetiological diagnosis, we designed a custom panel for sequencing coding regions from 40 genes known to be involved in the pathogenesis of CHA, using the Ion Torrent™ (Thermo Fisher Scientific, S.L. Waltham, MA, USA) Personal Genome Machine (PGM) Sequencer. A control group of 16 samples with previously known mutations and a test group of 10 patients with unknown mutations were included for assay validation and application, respectively. Results In the test group, we identified pathogenic mutations in all cases: four patients had novel mutations in genes related to membrane defects (SPTB, ANK1, SLC4A1 and EPB41), four were homozygous or compound heterozygous for mutations in genes related to enzyme deficiencies (GPI, TPI1 and GSS), one had a mutation in the HBB gene and another presented a homozygous mutation in the ADAMTS13 gene. Conclusions Ion PGM sequencing with our custom panel is a highly efficient way to detect mutations causing haemolytic anaemia, including new variations. It is a high‐throughput detection method that is ready for application in clinical laboratories.

show abstract

“…The sequence alignment is based on identifying structurally conserved regions (SCRs) common to the three templates. Three reference proteins are mannose-6-phosphate isomerase from C. albicans (1PMI) [13], mannose-6-phosphate isomerase from Bacillus subtilis (1QWR), and glucose-6-phosphate isomerase from Human (1JLH) [20]. The next step is to generate a multiple sequence alignment of human phosphomannose isomerase with the three templates.…”

Section: D Model Buildingmentioning

confidence: 99%

“…Three reference proteins, mannose-6-phosphate isomerase from C. albicans (1PMI) [13], mannose-6-phosphate isomerase from B. subtilis (1QWR), and glucose-6-phosphate isomerase from Human (1JLH) [20], were used to model the structure of human mannose-6-phosphate isomerase. The homology scores for the three reference proteins compared with hPMI were 40.9%, 23.2%, and 21.0%, respectively.…”

Section: Homology Modeling Of Hpmimentioning

confidence: 99%

Computational study of human phosphomannose isomerase: Insights from homology modeling and molecular dynamics simulation of enzyme bound substrate

Xiao

Guo

et al. 2006

Journal of Molecular Graphics and Modelling

View full text Add to dashboard Cite

Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps

Cited by 30 publications

References 16 publications

Bifunctional Phosphoglucose/Phosphomannose Isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum Constitute a Novel Enzyme Family within the Phosphoglucose Isomerase Superfamily

Bifunctional Phosphoglucose/Phosphomannose Isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum Constitute a Novel Enzyme Family within the Phosphoglucose Isomerase Superfamily

Detection of new pathogenic mutations in patients with congenital haemolytic anaemia using next‐generation sequencing

Computational study of human phosphomannose isomerase: Insights from homology modeling and molecular dynamics simulation of enzyme bound substrate

Contact Info

Product

Resources

About