The Enzyme Database

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EC 1.14.14.28     
Accepted name: long-chain alkane monooxygenase
Reaction: a long-chain alkane + FMNH2 + O2 = a long-chain primary alcohol + FMN + H2O
Systematic name: long-chain-alkane,FMNH2:oxygen oxidoreductase
Comments: The enzyme, characterized from the bacterium Geobacillus thermodenitrificans NG80-2, is capable of converting alkanes ranging from C15 to C36 into their corresponding primary alcohols [1,2]. The FMNH2 cofactor is provided by an FMN reductase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Feng, L., Wang, W., Cheng, J., Ren, Y., Zhao, G., Gao, C., Tang, Y., Liu, X., Han, W., Peng, X., Liu, R. and Wang, L. Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir. Proc. Natl. Acad. Sci. USA 104 (2007) 5602–5607. [PMID: 17372208]
2.  Li, L., Liu, X., Yang, W., Xu, F., Wang, W., Feng, L., Bartlam, M., Wang, L. and Rao, Z. Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. J. Mol. Biol. 376 (2008) 453–465. [PMID: 18164311]
3.  Dong, Y., Yan, J., Du, H., Chen, M., Ma, T. and Feng, L. Engineering of LadA for enhanced hexadecane oxidation using random- and site-directed mutagenesis. Appl. Microbiol. Biotechnol. 94 (2012) 1019–1029. [PMID: 22526792]
[EC 1.14.14.28 created 2016]
 
 


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