In-Silico Characterization and Homology Modeling of Catechol 1, 2 dioxygenase Involved in Processing of Catechol – an Intermediate of Aromatic Compound Degradation Pathway

α
Al-Hakim
Al-Hakim
σ
Mahmudul Hasan
Mahmudul Hasan
ρ
Rokib Hasan
Rokib Hasan
Ѡ
Md. Hazrat Ali
Md. Hazrat Ali
¥
Muhammad Fazle Rabbee
Muhammad Fazle Rabbee
§
Marufatuzzahan
Marufatuzzahan
χ
Hanif Mohammad Rejwan
Hanif Mohammad Rejwan
ν
Ziaul Faruque Joy
Ziaul Faruque Joy
α Shahjalal University of Science and Technology

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In-Silico Characterization and Homology Modeling of Catechol 1, 2 dioxygenase Involved in Processing of Catechol – an Intermediate of Aromatic Compound Degradation Pathway

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Abstract

Catechol 1, 2 dioxygenase (EC 1.13.11.1) is an enzyme intended to catalyze the degradation of catechol an intermediate of phenolic compound from ortho-mechanisms of the 3-oxoadipate pathway. Catechol 1, 2 dioxygenase plays a key role in the aerobic degradation of aromatic compounds, because it is the substrate for aromatic ring cleavage enzymes and as such it can be the starting point of many peripheral metabolic pathways. So, catechol 1, 2 dioxygenase is deliberated for a solution of environmental pollution occurred by aromatic compounds. In this study, we have focused on the in-silico characterization and homology modeling of catechol 1, 2 dioxygenase. The in silico analysis was performed by various computational tools and programmes. The physicochemical properties of the selected catechol 1, 2 dioxygenase were analyzed by using ExPASy’sProtParam tool and it was found that the molecular weight (M.Wt) ranges around 35000 Da. Isoelectric Points (pI) exhibits acidic nature and aliphatic index infers that 95% catechol 1, 2 dioxygenaseare stable. The negative value of GRAVY indicates that there will be better interaction with water. Motif analysis of the sequences was conducted by using MEME for predicting probable domain of catechol 1, 2-dioxygenase. Homology modeling of catechol 1, 2 dioxygenase taken from Pseudomonas aeruginosa MH38 (AC NO: CDH71767) was performed by I-TASSER. Various bioinformatics programmes and servers like RAMPAGE, PROCHECK and ERRAT were used for analysis and validation of final 3D structures created through homology modeling.

References

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Funding

No external funding was declared for this work.

Conflict of Interest

The authors declare no conflict of interest.

Ethical Approval

No ethics committee approval was required for this article type.

Data Availability

Not applicable for this article.

How to Cite This Article

Al-Hakim. 2015. \u201cIn-Silico Characterization and Homology Modeling of Catechol 1, 2 dioxygenase Involved in Processing of Catechol – an Intermediate of Aromatic Compound Degradation Pathway\u201d. Global Journal of Science Frontier Research - G: Bio-Tech & Genetics GJSFR-G Volume 15 (GJSFR Volume 15 Issue G1): .

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GJSFR Volume 15 Issue G1
Pg. 23- 33
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Crossref Journal DOI 10.17406/GJSFR

Print ISSN 0975-5896

e-ISSN 2249-4626

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GJSFR-G Classification: FOR Code: 060102
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v1.2

Issue date

October 17, 2015

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en
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Catechol 1, 2 dioxygenase (EC 1.13.11.1) is an enzyme intended to catalyze the degradation of catechol an intermediate of phenolic compound from ortho-mechanisms of the 3-oxoadipate pathway. Catechol 1, 2 dioxygenase plays a key role in the aerobic degradation of aromatic compounds, because it is the substrate for aromatic ring cleavage enzymes and as such it can be the starting point of many peripheral metabolic pathways. So, catechol 1, 2 dioxygenase is deliberated for a solution of environmental pollution occurred by aromatic compounds. In this study, we have focused on the in-silico characterization and homology modeling of catechol 1, 2 dioxygenase. The in silico analysis was performed by various computational tools and programmes. The physicochemical properties of the selected catechol 1, 2 dioxygenase were analyzed by using ExPASy’sProtParam tool and it was found that the molecular weight (M.Wt) ranges around 35000 Da. Isoelectric Points (pI) exhibits acidic nature and aliphatic index infers that 95% catechol 1, 2 dioxygenaseare stable. The negative value of GRAVY indicates that there will be better interaction with water. Motif analysis of the sequences was conducted by using MEME for predicting probable domain of catechol 1, 2-dioxygenase. Homology modeling of catechol 1, 2 dioxygenase taken from Pseudomonas aeruginosa MH38 (AC NO: CDH71767) was performed by I-TASSER. Various bioinformatics programmes and servers like RAMPAGE, PROCHECK and ERRAT were used for analysis and validation of final 3D structures created through homology modeling.

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In-Silico Characterization and Homology Modeling of Catechol 1, 2 dioxygenase Involved in Processing of Catechol – an Intermediate of Aromatic Compound Degradation Pathway

Al-Hakim
Al-Hakim Shahjalal University of Science and Technology
Mahmudul Hasan
Mahmudul Hasan
Rokib Hasan
Rokib Hasan
Md. Hazrat Ali
Md. Hazrat Ali
Muhammad Fazle Rabbee
Muhammad Fazle Rabbee
Marufatuzzahan
Marufatuzzahan
Hanif Mohammad Rejwan
Hanif Mohammad Rejwan
Ziaul Faruque Joy
Ziaul Faruque Joy

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