Analysis of Glyceraldehyde 3-Phosphate Dehydrogenase Gene in Lactarius Deliciosus Base on Bioinformatics

He Li; Guo Ying Zhou; Liang Guo; Ju Nang Liu

doi:10.4028/www.scientific.net/AMR.429.249

Paper Titles

Research on Energy Conversion Model of Solar Photovoltaic Power Generation System
p.222

Relationship of Flux Harmonics and Partitioning Method of Zero Voltage Vectors
p.229

Keywords Assignment to Fixed Image Region Segmentations Using Fuzzy SVMs
p.236

Efficient Antenna Selection in MIMO Correlated Channels
p.242

Analysis of Glyceraldehyde 3-Phosphate Dehydrogenase Gene in Lactarius Deliciosus Base on Bioinformatics
p.249

A Range Measurement Scheme for Chinese Terrestrial Television Broadcasting Signals Included Positioning Systems
p.253

Analysis of the Stability of Synchronous Motor Driving without Sensor
p.259

Study on Object Contour Extraction Based on Hölder Exponent and Multifractal Spectrum
p.267

An Improved Integrated Active Contour Model without Re-Initialization for Vector-Valued Images Segmentation
p.271

HomeAdvanced Materials ResearchAdvanced Materials Research Vol. 429Analysis of Glyceraldehyde 3-Phosphate...

Analysis of Glyceraldehyde 3-Phosphate Dehydrogenase Gene in Lactarius Deliciosus Base on Bioinformatics

Abstract:

Glyceraldehyde 3-phosphate dehydrogenase is an enzyme that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In the present study, some characters of the amino acid sequence of GAPDH of L.deliciosus were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 20 kinds of amino acid; the theoretical pI of GAPDH was 7.08 and the theoretical molecular weight of GAPDH was 26165.9 Da; the total number of atoms was 3714. It was a stable protein. There were 7 glycosylation sites and it was a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD (P) binding fold. C-terminal domain is a mixed alpha/antiparallel beta fold.

You might also be interested in these eBooks

View Preview

Info:

Periodical:

Advanced Materials Research (Volume 429)

Pages:

249-252

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.429.249

Citation:

Cite this paper

Online since:

January 2012

Authors:

He Li, Guo Ying Zhou, Liang Guo, Ju Nang Liu

Keywords:

Bioinformatic Analysis, GAPDH, L. deliciosus

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

References

[1] Gasteiger E., Hoogland C., Gattiker A., at al. (2005). Protein Identification and Analysis Tools on the ExPASy Server; (In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press. pp.571-607.

DOI: 10.1385/1-59259-890-0:571

Google Scholar

[2] Schwede T, Kopp J, Guex N, and Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research, 31: 3381-3385.

DOI: 10.1093/nar/gkg520

Google Scholar

[3] Marchler-Bauer A. (2009), CDD: specific functional annotation with the Conserved Domain Database., Nucleic Acids Res. 37(D)205-10.

Google Scholar

[4] Zheng L, Roeder RG, Luo Y (2003). S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component,. Cell 114 (2): 255–66.

DOI: 10.1016/s0092-8674(03)00552-x

Google Scholar

[5] Hara MR, Agrawal N, Kim SF, et al. (2005). S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding,. Nat. Cell Biol. 7 (7): 665–74.

DOI: 10.1038/ncb1268

Google Scholar

[6] Hara MR, Thomas B, Cascio MB, et al. (2006). Neuroprotection by pharmacologic blockade of the GAPDH death cascade,. Proc. Natl. Acad. Sci. U.S.A. 103 (10): 3887–9.

DOI: 10.1073/pnas.0511321103

Google Scholar