Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.15 - dihydropteroate synthase and Organism(s) Staphylococcus aureus and UniProt Accession O05701

for references in articles please use BRENDA:EC2.5.1.15
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase , while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus aureus
UNIPROT: O05701
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
dihydropteroate synthase, pfdhps, pvdhps, dihydropteroate synthetase, folp1, folp2, pvhppk-dhps, pppk-dhps, rv1207, hppk-dhps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7,8-dihydropteroate synthase
-
-
-
-
7,8-dihydropteroate synthetase
-
-
-
-
7,8-dihydropteroic acid synthetase
-
-
-
-
dihydropteroate diphosphorylase
-
-
-
-
dihydropteroate synthetase
-
-
-
-
dihydropteroic synthetase
-
-
-
-
synthase, dihydropteroate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(7,8-dihydropterin-6-yl)methyl diphosphate:4-aminobenzoate 2-amino-4-hydroxy-7,8-dihydropteridine-6-methenyltransferase
The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase [4], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9055-61-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
show the reaction diagram
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
show the reaction diagram
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
46% inhibition at 0.25 mM
N-(4-(trifluoromethyl)-benzylidene)-1-(4-(trifluoromethyl))benzylamine
-
complete inhibition at 0.25 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
Staphylococcus aureus
-
at pH 7.6 and 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
dihydropteroate synthase is the target of the sulfonamide class of drugs
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHPS_STAAU
267
0
29498
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E208K
mutation restores trimethoprim susceptibility closer to wild-type levels while further increasing sulfonamide resistance
F17L
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
S18L
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
T51M
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hampele, I.C.; D'Arcy, A.; Dale, G.E.; Kostrewa, D.; Nielsen, J.; Oefner, C.; Page, M.G.P.; Schonfeld, H.J.; Stuber, D.; Then, R.L.
Structure and function of the dihydropteroate synthase from Staphylococcus aureus
J. Mol. Biol.
268
21-30
1997
Staphylococcus aureus (O05701), Staphylococcus aureus
Manually annotated by BRENDA team
Hammoudeh, D.I.; Date, M.; Yun, M.K.; Zhang, W.; Boyd, V.A.; Viacava Follis, A.; Griffith, E.; Lee, R.E.; Bashford, D.; White, S.W.
Identification and characterization of an allosteric inhibitory site on dihydropteroate synthase
ACS Chem. Biol.
9
1294-1302
2014
Staphylococcus aureus, Yersinia pestis, Bacillus anthracis (Q81VW8)
Manually annotated by BRENDA team
Griffith, E.C.; Wallace, M.J.; Wu, Y.; Kumar, G.; Gajewski, S.; Jackson, P.; Phelps, G.A.; Zheng, Z.; Rock, C.O.; Lee, R.E.; White, S.W.
The structural and functional basis for recurring sulfa drug resistance mutations in Staphylococcus aureus dihydropteroate synthase
Front. Microbiol.
9
1369
2018
Staphylococcus aureus (O05701), Staphylococcus aureus
Manually annotated by BRENDA team