Literature summary extracted from

Jain, C.; Gupta, M.; Prasad, Y.; Wadhwa, G.; Sharma, S.
Homology modeling and protein engineering of alkane monooxygenase in Burkholderia thailandensis MSMB121 In silico insights (2014), J. Mol. Model., 20, 2340 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.14.28	-	Burkholderia thailandensis

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.14.28	homology modeling of the structure based on PDB entry 3B9N and molecular dynamics simulations	Burkholderia thailandensis

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.14.14.28	K361L	substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate	Burkholderia thailandensis
1.14.14.28	R359I	substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate	Burkholderia thailandensis
1.14.14.28	T369W	substitution in the IS4 region, resulting in improved binding energy. As the carbon chain increases the overall binding energy of alkane molecules from C30-C36 decreases as compared with C16. Mutated residue is not involved in binding sites but improves the accessibility of other residues towards the substrate	Burkholderia thailandensis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.14.28	Burkholderia thailandensis	-	-	-
1.14.14.28	Burkholderia thailandensis MSMB121	-	-	-

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Release 2023.1 (January 2023)