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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.
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: flavin-dependent monooxygenase RebC

Gene: rebC Accession Number: G-11522 (MetaCyc)

Synonyms: rbmD

Species: Lechevalieria aerocolonigenes

Summary:
RebC is a monomeric enzyme with three distinct domains. It binds a FAD cofactor, and has been characterized as a flavin-dependent monooxygenase [Ryan07]. The protein requires NADH for FAD reduction [HowardJones06].

The rebC gene was cloned into Escherichia coli and the protein was expressed as a His-tag fusion and purified [HowardJones06].

Upon flavin reduction, the RebC crystal undergoes a change in its unit cell dimension concurrent with a 5Å movement of the isoalloxazine ring, positioning the flavin ring adjacent to the substrate-binding pocket [Ryan08].

Gene Citations: [Sanchez02]

Molecular Weight of Polypeptide: 57.671 kD (from nucleotide sequence), 59.0 kD (experimental) [HowardJones06 ]

Unification Links: Protein Model Portal:Q8KI25 , SMR:Q8KI25 , UniProt:Q8KI25

Relationship Links: Entrez-Nucleotide:PART-OF:AF534707 , InterPro:IN-FAMILY:IPR002938 , InterPro:IN-FAMILY:IPR003042 , PDB:Structure:2R0C , PDB:Structure:2R0G , PDB:Structure:2R0P , PDB:Structure:3EPT , PDB:Structure:4EIP , PDB:Structure:4EIQ , Pfam:IN-FAMILY:PF01494 , Prints:IN-FAMILY:PR00420

Gene-Reaction Schematic: ?

Credits:
Created 09-Sep-2009 by Caspi R , SRI International


Enzymatic reaction of: flavin dependent hydroxylase (flavin-dependent monooxygenase RebC)

EC Number: 1.13.12.17

dichlorochromopyrrolate + 4 NADH + 4 oxygen + 6 H+ <=> dichloro-arcyriaflavin A + 2 CO2 + 4 NAD+ + 6 H2O

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: rebeccamycin biosynthesis

Cofactors or Prosthetic Groups: FAD [HowardJones06]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADH
138.0
[HowardJones06]


References

HowardJones06: Howard-Jones AR, Walsh CT (2006). "Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid." J Am Chem Soc 128(37);12289-98. PMID: 16967980

Ryan07: Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL (2007). "Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC." Proc Natl Acad Sci U S A 104(39);15311-6. PMID: 17873060

Ryan08: Ryan KS, Chakraborty S, Howard-Jones AR, Walsh CT, Ballou DP, Drennan CL (2008). "The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction." Biochemistry 47(51);13506-13. PMID: 19035832

Sanchez02: Sanchez C, Butovich IA, Brana AF, Rohr J, Mendez C, Salas JA (2002). "The biosynthetic gene cluster for the antitumor rebeccamycin: characterization and generation of indolocarbazole derivatives." Chem Biol 9(4);519-31. PMID: 11983340


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 Sat Dec 20, 2014, BIOCYC14B.