Literature: Dihydropteroate synthase-like (IPR011005)
References used in this entry
The following publications were referred to in the abstract:
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
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
The following publications were not referred to in the abstract, but provide useful additional information:
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
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
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