New simulated 3d-structure catalytic sites prediction for desacetoxyvindoline4-hydroxylase flavanone 3- hydroxylase and hyoscyamine 6--hydroxylase


Citation

Ong Lisa Gaik Ai, . and Goh Khang Wen, . and Chan Mun Yee, . and Wong Yong Seng, . and Chin Hong Soon, . and Teo Kah Cheng, . (2011) New simulated 3d-structure catalytic sites prediction for desacetoxyvindoline4-hydroxylase flavanone 3- hydroxylase and hyoscyamine 6--hydroxylase. [Proceedings Paper]

Abstract

Enzymes play an important role in our life leading to many contributions for different industrial fields. Protein functions are mainly determined by their structure. Although most enzyme sequences have been determined the corresponding X-ray crystallography structures however are lacking. Experimental 3-dimensional 3D structure determination methods such as X-ray crystallography or nuclear magnetic resonance techniques are time consuming and complicated. Therefore simulated 3D structures of unknown enzymes allow their catalytic sites to be predicted. Besides that the conserved motif for the substrate cofactor and iron binding site for each of the modeled enzyme can also be determined. Furthermore the 3D structures of proteins can be validated using PROCHECK to ensure that the quality of the protein structures with G-factor greater than -0.5 are achieved. Finally this comparative modeling enzyme method will be the alternative way to predict the 3D-structures for those proteins with unknown structures.


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Abstract

Enzymes play an important role in our life leading to many contributions for different industrial fields. Protein functions are mainly determined by their structure. Although most enzyme sequences have been determined the corresponding X-ray crystallography structures however are lacking. Experimental 3-dimensional 3D structure determination methods such as X-ray crystallography or nuclear magnetic resonance techniques are time consuming and complicated. Therefore simulated 3D structures of unknown enzymes allow their catalytic sites to be predicted. Besides that the conserved motif for the substrate cofactor and iron binding site for each of the modeled enzyme can also be determined. Furthermore the 3D structures of proteins can be validated using PROCHECK to ensure that the quality of the protein structures with G-factor greater than -0.5 are achieved. Finally this comparative modeling enzyme method will be the alternative way to predict the 3D-structures for those proteins with unknown structures.

Additional Metadata

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Item Type: Proceedings Paper
Additional Information: Available at Perpustakaan Sultan Abdul Samad Universiti Putra Malaysia 43400 UPM Serdang Selangor Malaysia. QR22 M3I61 2011 vol.2 Call Number.
AGROVOC Term: Enzymes
AGROVOC Term: Proteins
AGROVOC Term: Catalytic activity
AGROVOC Term: Hyoscyamine
AGROVOC Term: Prediction
AGROVOC Term: Nucleotide sequence
AGROVOC Term: Amino acid sequences
AGROVOC Term: Simulation models
AGROVOC Term: Protein quality
AGROVOC Term: Microstructure morphology
Geographical Term: MALAYSIA
Depositing User: Ms. Suzila Mohamad Kasim
Last Modified: 24 Apr 2025 05:15
URI: http://webagris.upm.edu.my/id/eprint/12909

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