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Literature: Dihydropteroate synthase-like (IPR011005)

References used in this entry

• The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase.
  Volpe F, Dyer M, Scaife JG, Darby G, Stammers DK, Delves CJ.
  Gene 112 213-8 1992
  PMID: 1313386 Related citations
• Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action.
  Baca AM, Sirawaraporn R, Turley S, Sirawaraporn W, Hol WG.
  J. Mol. Biol. 302 1193-212 2000
  PMID: 11007651 Related citations
• Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
  Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW.
  Structure 8 817-30 2000
  PMID: 10997901 Related citations
• Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase.
  Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK.
  Nat. Struct. Biol. 4 490-7 1997
  PMID: 9187658 Related citations

Further reading

• Dihydropteroate synthase from Streptococcus pneumoniae: structure, ligand recognition and mechanism of sulfonamide resistance.
  Levy C, Minnis D, Derrick JP.
  Biochem. J. 412 379-88 2008
  PMID: 18321242 Related citations
• Metal active site elasticity linked to activation of homocysteine in methionine synthases.
  Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML.
  Proc. Natl. Acad. Sci. U.S.A. 105 3286-91 2008
  PMID: 18296644 Related citations
• The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae.
  Lawrence MC, Iliades P, Fernley RT, Berglez J, Pilling PA, Macreadie IG.
  J. Mol. Biol. 348 655-70 2005
  PMID: 15826662 Related citations
• Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
  Evans JC, Huddler DP, Hilgers MT, Romanchuk G, Matthews RG, Ludwig ML.
  Proc. Natl. Acad. Sci. U.S.A. 101 3729-36 2004
  PMID: 14752199 Related citations
• Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.
  Doukov TI, Hemmi H, Drennan CL, Ragsdale SW.
  J. Biol. Chem. 282 6609-18 2007
  PMID: 17172470 Related citations