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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Enzyme: 1-deoxypentalenate 11-hydroxylase

Gene: ptlH Accession Numbers: G-14661 (MetaCyc), SAV_2991

Species: Streptomyces avermitilis

Summary:
The ptlH gene from the pentalenolactone gene cluster of Streptomyces avermitilis encodes 1-deoxypentalenate 11-hydroxylase, an enzyme that catalyzes the Fe(II)- and 2-ketoglutarate-dependent hydroxylation of 1-deoxypentalenate to 1-deoxy-11β-hydroxypentalenate, a step in the biosynthesis of the sesquiterpenoid antibiotic compound pentalenolactone. The enzyme is a non-heme iron dioxygenase

The gene was cloned by PCR and expressed in Escherichia coli as an N-terminal His6-tag protein, and the recombinant protein was purified [You06].

The x-ray crystal structure of PtlH was determined in several complexes with the cofactors iron, 2-ketoglutarate, and the non-reactive enantiomer of the substrate, ent-1-deoxypentalenate [You07].

Gene Citations: [Omura01]

Molecular Weight of Polypeptide: 32.264 kD (from nucleotide sequence)

Unification Links: Entrez-gene:1210627 , Protein Model Portal:Q82IZ1 , SMR:Q82IZ1 , String:227882.SAV_2991 , UniProt:Q82IZ1

Relationship Links: InterPro:IN-FAMILY:IPR008775 , PDB:Structure:2RDN , PDB:Structure:2RDQ , PDB:Structure:2RDR , PDB:Structure:2RDS , Pfam:IN-FAMILY:PF05721

Gene-Reaction Schematic: ?

Credits:
Created 26-Sep-2011 by Caspi R , SRI International


Enzymatic reaction of: 1-deoxypentalenate 11-hydroxylase

EC Number: 1.14.11.35

1-deoxypentalenate + 2-oxoglutarate + oxygen <=> 1-deoxy-11β-hydroxypentalenate + succinate + CO2

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: neopentalenoketolactone and pentalenate biosynthesis

Cofactors or Prosthetic Groups: Fe2+

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
1-deoxypentalenate
570.0
4.2
[You06]

pH(opt): 6 [You06]


References

Omura01: Omura S, Ikeda H, Ishikawa J, Hanamoto A, Takahashi C, Shinose M, Takahashi Y, Horikawa H, Nakazawa H, Osonoe T, Kikuchi H, Shiba T, Sakaki Y, Hattori M (2001). "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Proc Natl Acad Sci U S A 98(21);12215-20. PMID: 11572948

You06: You Z, Omura S, Ikeda H, Cane DE (2006). "Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis." J Am Chem Soc 128(20);6566-7. PMID: 16704250

You07: You Z, Omura S, Ikeda H, Cane DE, Jogl G (2007). "Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis." J Biol Chem 282(50);36552-60. PMID: 17942405


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 Sun Dec 21, 2014, BIOCYC13B.