Enzyme

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     2. Transferases
        2.5 Transferring alkyl or aryl groups, other than methyl groups
            2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
ID:2.5.1.15
Description:Dihydropteroate synthase.
Alternative Name: Dihydropteroate pyrophosphorylase.
Dihydropteroate diphosphorylase.
DHPS.
Prosite: PDOC50972; PDOC00630;
PDB:
PDBScop
1EYE 8031491; 8043869;
6CLV 8031488; 8043866; 8031488; 8043866; 8031488; 8043866; 8031488; 8043866;
6CLU 8031488; 8043866; 8031488; 8043866; 8031488; 8043866; 8031488; 8043866;
1AD4 8031488; 8043866; 8031488; 8043866;
1AD1 8031488; 8043866; 8031488; 8043866;
 » show all

Cath: 3.20.20.20; 3.30.1130.10; 3.30.1300.20; 3.30.70.560;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.5.1.15
BRENDA Enzyme Link: BRENDA 2.5.1.15
KEGG Enzyme Link: KEGG2.5.1.15
BioCyc Enzyme Link: BioCyc 2.5.1.15
ExPASy Enzyme Link: ExPASy2.5.1.15
EC2PDB Enzyme Link: EC2PDB 2.5.1.15
ExplorEnz Enzyme Link: ExplorEnz 2.5.1.15
PRIAM enzyme-specific profiles Link: PRIAM 2.5.1.15
IntEnz Enzyme Link: IntEnz 2.5.1.15
MEDLINE Enzyme Link: MEDLINE 2.5.1.15
MSA:

2.5.1.15;

Phylogenetic Tree:

2.5.1.15;

Uniprot:
M-CSA:
RHEA:19949 (7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[O;H0;+0:4]-[CH2;+0:5]-[*:6]>>[*:1]-[NH;+0:2]-[CH2;+0:5]-[*:6].[*:3]-[OH;+0:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Structure and function of the dihydropteroate synthase from Staphylococcus aureus.Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schönfeld HJ, Stüber D, Then RL1997 Apr 259149138
Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localized in mitochondria.Rébeillé F, Macherel D, Mouillon JM, Garin J, Douce R1997 Mar 39118956
The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase.Volpe F, Ballantine SP, Delves CJ1993 Sep 18397083
The hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii expressed as an independent enzyme in Escherichia coli: refolding and characterization of the recombinant enzyme.Ballantine SP, Volpe F, Delves CJ1994 Aug7950384
Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii.Volpe F, Ballantine SP, Delves CJ1995 Jul 47543066
Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis.Chakraborty S, Gruber T, Barry CE 3rd, Boshoff HI, Rhee KY2013 Jan 423118010
Characterization of a novel bifunctional dihydropteroate synthase/dihydropteroate reductase enzyme from Helicobacter pylori.Levin I, Mevarech M, Palfey BA2007 Jun17416665
Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response.Storozhenko S, Navarrete O, Ravanel S, De Brouwer V, Chaerle P, Zhang GF, Bastien O, Lambert W, Rébeillé F, Van Der Straeten D2007 Apr 617289662
Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli.Nopponpunth V, Sirawaraporn W, Greene PJ, Santi DV1999 Nov10542185
Dihydropteroate synthase from Streptococcus pneumoniae: characterization of substrate binding order and sulfonamide inhibition.Vinnicombe HG, Derrick JP1999 May 1910329458
Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100.Talarico TL, Dev IK, Dallas WS, Ferone R, Ray PH1991 Nov1657875
Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth.Güldener U, Koehler GJ, Haussmann C, Bacher A, Kricke J, Becher D, Hegemann JH2004 Aug15169867