Gene Symbol: moaD
Description: molybdopterin synthase, small subunit
Alias: ECK0773, JW0767, chlM
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Gutzke G, Fischer B, Mendel R, Schwarz G. Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins. J Biol Chem. 2001;276:36268-74 pubmed
    ..2000) Nat. Struct. Biol. 8, 42-46) shows the heterotetrameric nature of the enzyme that is composed of two small (MoaD) and two large subunits (MoaE)...
  2. Taylor J, Bedbrook J, Grant F, Kleinhofs A. Reconstitution of plant nitrate reductase by Escherichia coli extracts and the molecular cloning of the chlA gene of Escherichia coli K12. J Mol Appl Genet. 1983;2:261-71 pubmed
    ..This suggested that the chlA gene was contained intact, including its own promoter, on the 1.9 kb BclI fragment. ..
  3. Pitterle D, Rajagopalan K. The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor. J Biol Chem. 1993;268:13499-505 pubmed
  4. Wuebbens M, Rajagopalan K. Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. J Biol Chem. 2003;278:14523-32 pubmed
    ..for adding the dithiolene to a desulfo precursor termed precursor Z, is a dimer of dimers containing the MoaD and MoaE proteins...
  5. Schmitz J, Wuebbens M, Rajagopalan K, Leimkuhler S. Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry. 2007;46:909-16 pubmed
    In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis...
  6. Lake M, Wuebbens M, Rajagopalan K, Schindelin H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature. 2001;414:325-9 pubmed
    ..The Escherichia coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis, an evolutionarily conserved pathway...
  7. Zhang W, Urban A, Mihara H, Leimkuhler S, Kurihara T, Esaki N. IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. J Biol Chem. 2010;285:2302-8 pubmed publisher
    ..In molybdenum cofactor biosynthesis, MoeB activates the C terminus of the MoaD subunit of molybdopterin (MPT) synthase to form MoaD-adenylate, which is subsequently converted to a ..
  8. Rudolph M, Wuebbens M, Turque O, Rajagopalan K, Schindelin H. Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. J Biol Chem. 2003;278:14514-22 pubmed of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE) and small (MoaD) subunit...
  9. Shanmugam K, Stewart V, Gunsalus R, Boxer D, Cole J, Chippaux M, et al. Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Salmonella typhimurium. Mol Microbiol. 1992;6:3452-4 pubmed

More Information


  1. Rivers S, McNairn E, Blasco F, Giordano G, Boxer D. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol Microbiol. 1993;8:1071-81 pubmed
    ..mutants, which have been biochemically characterized as defective in molybdopterin biosynthesis, indicates that these carry lesions in moaA and moaD respectively. The moa locus is orientated clockwise at 17.7 minutes in the chromosome.
  2. McNicholas P, Rech S, Gunsalus R. Characterization of the ModE DNA-binding sites in the control regions of modABCD and moaABCDE of Escherichia coli. Mol Microbiol. 1997;23:515-24 pubmed
    ..These findings demonstrate that ModE acts both as a repressor and activator of the mod and moa operons, respectively, depending on the properties of the binding site. ..
  3. Tong Y, Wuebbens M, Rajagopalan K, Fitzgerald M. Thermodynamic analysis of subunit interactions in Escherichia coli molybdopterin synthase. Biochemistry. 2005;44:2595-601 pubmed
    The molybdopterin (MPT) synthase complex in Escherichia coli consists of two MoaE subunits and two MoaD subunits in a heterotetrameric structure with the two MoaE subunits forming a central dimer...
  4. Johnson M, Rajagopalan K. Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis. J Bacteriol. 1987;169:117-25 pubmed
    ..genetic complementation groups from previously isolated chlA and chlE mutations and have been designated as chlM and chlN (closely linked to chlA and chlE, respectively)...
  5. Rudolph M, Wuebbens M, Rajagopalan K, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 2001;8:42-6 pubmed
    ..The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway. ..
  6. Leimkuhler S, Wuebbens M, Rajagopalan K. Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J Biol Chem. 2001;276:34695-701 pubmed
    ..of Escherichia coli MoeB suggested that the MoeB-dependent formation of a C-terminal thiocarboxylate on the MoaD subunit of molybdopterin synthase might resemble the ubiquitin-activating step in the ubiquitin-targeted ..
  7. Leimkuhler S, Rajagopalan K. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 2001;276:22024-31 pubmed
    ..A comparison of the ability of the three sulfurtransferases to provide the sulfur for MPT formation showed the highest activity for CSD in the in vitro system. ..
  8. Rajagopalan K. Biosynthesis and processing of the molybdenum cofactors. Biochem Soc Trans. 1997;25:757-61 pubmed