Literature summary for 1.14.14.28 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 .

Search for more literature for 1.14.14.28

Cloned(Commentary)

Cloned (Comment)	Organism
-	Burkholderia thailandensis

Crystallization (Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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
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

Organism	UniProt	Comment	Textmining
Burkholderia thailandensis	-	-	-
Burkholderia thailandensis MSMB121	-	-	-

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Release 2023.1 (January 2023)