MetaCyc Polypeptide: alkane 1-monooxygenase

Gene: alkB Accession Number: G-2902 (MetaCyc)

Synonyms: alkane omega-hydroxylase

Species: Pseudomonas oleovorans

Component of: alkane hydroxylase system (summary available)

Alkane hydroxylase is a component of the alkane hydoxylase system, which catalyzes the first oxidation step in alkane utilization.
The alk genes of P. putida GP01 (formerly known as P. alevorans) are located in two clusters on the large OCT plasmid. One cluster contains the genes alkBFGHJKL, while the other cluster contains alkT and alkS. The alkB gene was identified and sequenced by Kok et al [Rougraff89].

Gene Citations: [Kok89]

Locations: inner membrane

Molecular Weight of Polypeptide: 45.806 kD (from nucleotide sequence), 41 kD (experimental) [Kok89a ]

Unification Links: Protein Model Portal:P12691 , UniProt:P12691

Relationship Links: Entrez-Nucleotide:RELATED-TO:AJ245436 , InterPro:IN-FAMILY:IPR005804 , Pfam:IN-FAMILY:PF00487

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Cellular Component: GO:0005886 - plasma membrane

MultiFun Terms: metabolism carbon utilization

Subunit of: alkane hydroxylase system

Species: Pseudomonas oleovorans

Subunit composition of alkane hydroxylase system = [AlkB][AlkG][AlkT]
         alkane 1-monooxygenase = AlkB (summary available)
         rubredoxin 2 = AlkG (summary available)
         rubredoxin-NAD(+) reductase = AlkT (extended summary available)

The Pseudomonas oleovorans alkane hydroxylase system system is encoded on a plasmid, and composed of three components. alkane 1-monooxygenase, the catalytic component, is an integral membrane protein that contains non-heme ferrous iron. It transfers one oxygen atom from molecular oxygen into the terminal carbon atom of (C6 to C12) aliphatic hydrocarbons [Ueda72] yielding a primary alcohol [Chen95a]. The other oxygen atom is reduced with electrons supplied by the NADH-dependent rubredoxin-NAD(+) reductase, via the electron carrier rubredoxin 2.

The purified enzyme has a wide range of substrates, and can accept linear alkanes up to n-dodecane (although in vivo activity seems to be limited to n-decane). The enzyme can also accept branched alkanes and alicyclic compounds [vanBeilen94]

[Ueda72, Ueda72a, Staijen00, vanBeilen92, Ruettinger77, Ruettinger74].

Locations: inner membrane

GO Terms:

Cellular Component: GO:0005886 - plasma membrane [Kok89a]

Created 16-Aug-2004 by Caspi R , SRI International

Enzymatic reaction of: alkane hydroxylase

EC Number:

n-octane + 2 a reduced rubredoxin + oxygen + 2 H+ <=> 1-octanol + 2 an oxidized rubredoxin + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for n-octane: m-xylene [vanBeilen94 ] , p-xylene [vanBeilen94 ] , n-hexane [vanBeilen94 ] , n-undecane [vanBeilen94 ] , n-dodecane [vanBeilen94 ] , n-nonane [vanBeilen94 ] , n-pentane [vanBeilen94 ] , n-heptane [vanBeilen94 ] , n-decane [vanBeilen94 ]

In Pathways: octane oxidation

Cofactors or Prosthetic Groups: Fe2+ [vanBeilen94]


Chen95a: Chen Q, Janssen DB, Witholt B (1995). "Growth on octane alters the membrane lipid fatty acids of Pseudomonas oleovorans due to the induction of alkB and synthesis of octanol." J Bacteriol 177(23);6894-901. PMID: 7592483

Kok89: Kok M, Oldenhuis R, van der Linden MP, Meulenberg CH, Kingma J, Witholt B (1989). "The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase." J Biol Chem 264(10);5442-51. PMID: 2647719

Kok89a: Kok M, Oldenhuis R, van der Linden MP, Raatjes P, Kingma J, van Lelyveld PH, Witholt B (1989). "The Pseudomonas oleovorans alkane hydroxylase gene. Sequence and expression." J Biol Chem 264(10);5435-41. PMID: 2647718

Rougraff89: Rougraff PM, Zhang B, Kuntz MJ, Harris RA, Crabb DW (1989). "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases." J Biol Chem 264(10);5899-903. PMID: 2647728

Ruettinger74: Ruettinger RT, Olson ST, Boyer RF, Coon MJ (1974). "Identification of the omega-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein requiring phospholipid for catalytic activity." Biochem Biophys Res Commun 1974;57(4);1011-7. PMID: 4830742

Ruettinger77: Ruettinger RT, Griffith GR, Coon MJ (1977). "Characterization of the omega-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein." Arch Biochem Biophys 1977;183(2);528-37. PMID: 921275

Staijen00: Staijen IE, Van Beilen JB, Witholt B (2000). "Expression, stability and performance of the three-component alkane mono-oxygenase of Pseudomonas oleovorans in Escherichia coli." Eur J Biochem 2000;267(7);1957-65. PMID: 10727934

Ueda72: Ueda T, Coon MJ (1972). "Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation." J Biol Chem 1972;247(16);5010-6. PMID: 4403503

Ueda72a: Ueda, T, Lode, ET, Coon, MJ (1972). "Enzymatic ω-Oxidation VI. Isolation of homogeneous reduced diphosphopyridine nucleotide-rubredoxin reductase." The Journal of Biological Chemistry 247:2109-2116.

vanBeilen92: van Beilen JB, Penninga D, Witholt B (1992). "Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans." J Biol Chem 1992;267(13);9194-201. PMID: 1315749

vanBeilen94: van Beilen, J. B. (1994). "Alkane oxidation by Pseudomonas oleovorans: genes and proteins." Ph.D. thesis, University of Groningen.

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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