Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: hydroxyneurosporene methyltransferase

Gene: crtF Accession Number: G-11383 (MetaCyc)

Synonyms: 1-hydroxycarotenoid methylase

Species: Rhodobacter capsulatus

Summary:
The subunit structure of this enzyme has not been reported.

This enzyme from the purple non-sulfur bacterium Rhodobacter capsulatus catalyzes the S-adenosyl-L-methionine-dependent O-methylation of the 1-hydroxy group of several acyclic carotenoids which function in the photosynthetic apparatus of this organism. Its enzymatic function was shown by complementation studies in an Escherichia coli host transformed with carotenogenic plasmids. The recombinant enzyme from Rhodobacter capsulatus was also overexpressed in Escherichia coli, purified and characterized [Badenhop03].

Gene Citations: [Armstrong89]

Molecular Weight of Polypeptide: 43.039 kD (from nucleotide sequence)

Unification Links: Protein Model Portal:P0CY89 , UniProt:P0CY89

Relationship Links: Entrez-Nucleotide:PART-OF:X52291 , InterPro:IN-FAMILY:IPR001077 , Pfam:IN-FAMILY:PF00891 , Prosite:IN-FAMILY:PS51683

Gene-Reaction Schematic: ?

Credits:
Created 25-Jun-2009 by Caspi R , SRI International
Revised 10-Sep-2010 by Fulcher CA , SRI International


Enzymatic reaction of: demethylspheroidene methyltransferase (hydroxyneurosporene methyltransferase)

EC Number: 2.1.1.210

demethylspheroidene + S-adenosyl-L-methionine <=> spheroidene + S-adenosyl-L-homocysteine + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: spheroidene and spheroidenone biosynthesis

Summary:
The purified, recombinant enzyme showed a broad substrate specificity for 1-hydroxy carotenoids. It utilized S-adenosyl-L-homocysteine as the only cofactor [Badenhop03].


Enzymatic reaction of: hydroxyneurosporene methyltransferase

EC Number: 2.1.1.-

1-hydroxyneurosporene + S-adenosyl-L-methionine <=> methoxyneurosporene + S-adenosyl-L-homocysteine + H+

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.

In Pathways: spheroidene and spheroidenone biosynthesis

Summary:
The purified, recombinant enzyme showed a broad substrate specificity for 1-hydroxy carotenoids. It utilized S-adenosyl-L-homocysteine as the only cofactor [Badenhop03].


References

Armstrong89: Armstrong GA, Alberti M, Leach F, Hearst JE (1989). "Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus." Mol Gen Genet 216(2-3);254-68. PMID: 2747617

Badenhop03: Badenhop F, Steiger S, Sandmann M, Sandmann G (2003). "Expression and biochemical characterization of the 1-HO-carotenoid methylase CrtF from Rhodobacter capsulatus." FEMS Microbiol Lett 222(2);237-42. PMID: 12770713

Scolnik80: Scolnik PA, Walker MA, Marrs BL (1980). "Biosynthesis of carotenoids derived from neurosporene in Rhodopseudomonas capsulata." J Biol Chem 255(6);2427-32. PMID: 7358679


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC14A.