Enzymatic activation of alkanes: constraints and prospective

Ayala, Marcela; Torres, Eduardo

doi:10.1016/j.apcata.2004.05.046

Cited by 77 publications

(59 citation statements)

References 105 publications

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“…As enzyme molecules alone or in combination with drugs, antibodies and antigens, are the most used in industries, we will be focusing on the immobilization techniques used for enzymes as a model of other immobilized molecules. The enzyme market in 2005 was around 2.65 billion dollars, with an expected annual growth of more than 9% [6]. On the industrial level, 75% of the enzymes were used, which is around 2 billion dollars.…”

Section: Methods Of Immobilizationmentioning

confidence: 99%

Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology

Elnashar¹

2010

JBNB

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Section: Methods Of Immobilizationmentioning

confidence: 99%

Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology

Elnashar¹

2010

JBNB

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“…They contain enzyme systems like the diiron-and copper-containing methane monooxygenases found in many methanotrophs, such as Methylococcus capsulatus (Bath) (24), integral membrane-bound diiron AlkB proteins present in many ␣, ␤, and ␥-proteobacteria and high-GϩC-content gram-positive bacteria (40), and membranebound heme-containing cytochrome P450 enzymes (CYP) found in many alkane-degrading yeasts and fungi (3,9,36).…”

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confidence: 99%

CYP153A6, a Soluble P450 Oxygenase Catalyzing Terminal-Alkane Hydroxylation

et al. 2006

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The first and key step in alkane metabolism is the terminal hydroxylation of alkanes to 1-alkanols, a reaction catalyzed by a family of integral-membrane diiron enzymes related to Pseudomonas putida GPo1 AlkB, by a diverse group of methane, propane, and butane monooxygenases and by some membrane-bound cytochrome P450s. Recently, a family of cytoplasmic P450 enzymes was identified in prokaryotes that allow their host to grow on aliphatic alkanes. One member of this family, CYP153A6 from Mycobacterium sp. HXN-1500, hydroxylates medium-chain-length alkanes (C 6 to C 11 ) to 1-alkanols with a maximal turnover number of 70 min ؊1 and has a regiospecificity of >95% for the terminal carbon atom position. Spectroscopic binding studies showed that C 6 -to-C 11 aliphatic alkanes bind in the active site with K d values varying from ϳ20 nM to 3.7 M. Longer alkanes bind more strongly than shorter alkanes, while the introduction of sterically hindering groups reduces the affinity. This suggests that the substrate-binding pocket is shaped such that linear alkanes are preferred. Electron paramagnetic resonance spectroscopy in the presence of the substrate showed the formation of an enzyme-substrate complex, which confirmed the binding of substrates observed in optical titrations. To rationalize the experimental observations on a molecular scale, homology modeling of CYP153A6 and docking of substrates were used to provide the first insight into structural features required for terminal alkane hydroxylation.

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“…As enzyme molecules alone or in combination with drugs, antibodies and antigens, are the most used in industries, we will be focusing on the immobilization techniques used for enzymes as a model of other immobilized molecules. The enzyme market in 2005 was around 2.65 billion dollars, with an expected annual growth of more than 9% (Ayala and Torres, 2004). On the industrial level, 75% of the enzymes were used, which is around 2 billion dollars.…”

Section: Methods Of Immobilizationmentioning

confidence: 99%

The Art of Immobilization Using Biopolymers, Biomaterials and Nanobiotechnology

Elnashar¹

2011

Biotechnology of Biopolymers

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Enzymatic activation of alkanes: constraints and prospective

Cited by 77 publications

References 105 publications

Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology

Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology

CYP153A6, a Soluble P450 Oxygenase Catalyzing Terminal-Alkane Hydroxylation

The Art of Immobilization Using Biopolymers, Biomaterials and Nanobiotechnology

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