Any feedback?
Information on EC 2.7.7.60 - 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
for references in articles please use BRENDA:EC2.7.7.60Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.60 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferaseIUBMB Comments
The enzyme from Escherichia coli requires Mg2+ or Mn2+. ATP or UTP can replace CTP, but both are less effective. GTP and TTP are not substrates. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Specify your search results
Word Map
- 2.7.7.60
- phosphatidylcholine
-
ctp:phosphocholine
- phospholipid
- phosphocholine
- phosphatidylethanolamine
- cdp-choline
- cytidine
-
2.7.7.15
-
cholinephosphate
- phosphatidylglycerol
-
cholinephosphotransferase
-
3hcholine
-
ptdcho
- cctalpha
-
disaturated
- cdp-ethanolamine
-
ctp:cholinephosphate
-
h-form
-
cmp-kdo
-
ctp:phosphatidic
- analysis
- drug development
-
ctp:phosphoethanolamine
- medicine
- biotechnology
-
cytidylylation
- pcyt1a
-
vance
-
methyl-3hcholine
-
cytidylytransferase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cytidylyltransferase, pfispd, 2-c-methyl-d-erythritol 4-phosphate cytidylyltransferase, aamct, mtispd, mep cytidylyltransferase, 2-c-methyl-d-erythritol-4-phosphate cytidyltransferase, 4-diphosphocytidyl-2c-methyl-d-erythritol synthase, cdp-me synthetase, 2c-methyl-d-erythritol-4-phosphate cytidylyltransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-C-methyl erythritol 4-phosphate cytidylyltransferase
-
-
-
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
2-C-methyl-D-erythritol-4-phosphate cytidyltransferase
2-C-methyl-D-erythritol-4-phosphate cytidylyltransferase
-
-
-
-
2-C-methylerythritol 4-cytidylyltransferase
-
-
-
-
2C-methyl-D-erythritol-4-phosphate cytidylyltransferase
4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase
-
-
-
-
4-diphosphocytidyl-2-C-methylerythritol synthase
-
-
-
-
4-diphosphocytidyl-2C-methyl-D-erythritol synthase
-
-
-
-
BsIspD
CDP-ME synthetase
-
-
-
-
CDPME synthetase
CMS
CTP:2-C-methyl-D-erythritol-4-phosphate cytidylyltransferase synthetase
-
-
cytidylyltransferase, 2-C-methylerythritol 4-
-
-
-
-
FtIspD
IspD
IspDF
MCT
MEP cytidyltransferase
MEP cytidylyltransferase
MtIspD
PlIspD
PvIspD
PVX_081425
Rv3582c
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Plasmodium falciparum Tanzania (20000708)
-
-
IspDF
-
bifunctional enzyme catalyzing non-consecutive reactions in the 1-deoxy-D-xylulose 5-phosphate pathway of isoprenoid precursor biosynthesis
IspDF
-
bifunctional enzyme catalyzing non-consecutive reactions in the 1-deoxy-D-xylulose 5-phosphate pathway of isoprenoid precursor biosynthesis
MCT
-
-
-
-
MEP cytidylyltransferase
-
-
-
-
MtIspD
-
ispD gene from Mycobacterium tuberculosis H37Rv, Rv3582c
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ordered sequential mechanism
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
cytidyltransferase family. Active substrate site consists of a glycine-rich loop spanning Pro13-Arg20. Three-dimensional structure of enzyme is figured out
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
The enzyme from Escherichia coli requires Mg2+ or Mn2+. ATP or UTP can replace CTP, but both are less effective. GTP and TTP are not substrates. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis
-
-
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
no kinetic evidence for substrate channelling
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
third step in MEP pathway, isoprenoid biosynthesis
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
conformational change of P-loop in the catalysis, concerted movements of the P-loop and L2-loop may be essential during the catalytic reaction, modeling
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
IspD of Escherichia coli (EcIspD) follows stereochemical principles underlying the catalysis mechanism
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
conformational change of P-loop in the catalysis, concerted movements of the P-loop and L2-loop may be essential during the catalytic reaction, modeling
-
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
conformational change of P-loop in the catalysis, concerted movements of the P-loop and L2-loop may be essential during the catalytic reaction, modeling
Bacillus subtilis DSM 23778
-
-
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
third step in MEP pathway, isoprenoid biosynthesis
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
The enzyme from Escherichia coli requires Mg2+ or Mn2+. ATP or UTP can replace CTP, but both are less effective. GTP and TTP are not substrates. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
251990-59-7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
-
13% activity compared to CTP as substrate, 30°C, 15 min, pH8
-
-
?
2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
-
13% activity compared to CTP as substrate, 30°C, 15 min, pH8
-
-
?
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
30°C, 15 min, pH8
coupled to hydrolysis of diphosphate to phosphate followed by complex formation with ammonium molybdate-malachite green (absorbance at 630 nm)
-
?
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
30°C, 15 min, pH8
coupled to hydrolysis of diphosphate to phosphate followed by complex formation with ammonium molybdate-malachite green (absorbance at 630 nm)
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
ATP, UTP, GTP, ITP, dTTP, dGTP, dCTP ann dATP tested as substrates besides CTP
-
r
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Bacillus subtilis DSM 23778
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
r
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in he mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Francisella tularensis subsp. novicida Utah 112
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Plasmodium falciparum Tanzania (20000708)
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
additional information
?
-
-
lipoate-protein ligase attaches octanoate to the dehydrogenase subunit and sulfur insertion protein LipA then converts octanoate to lipoate. LipA acts on both octanoate and octanoyl-proteins
-
-
?
additional information
?
-
-
using an assay method for determination of the catalytic activity measuring the production of radiolabeled 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 14C-labeled 2-C-methyl-D-erythritol 4-phosphate, and separation of non-radioactive 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from CTP by C18 reverse phase HPLC with a mobile phase of 0.1 M ammonium bicarbonate (98%) and acetonitrile (2%) at pH 7.4
-
-
?
additional information
?
-
-
GTP, UTP and ITP are no substrates
-
-
?
additional information
?
-
-
GTP, UTP and ITP are no substrates
-
-
?
additional information
?
-
substrate molecular docking study, binding site mapping and analysis
-
-
-
additional information
?
-
the fluorimetric assay directly measures diphosphate
-
-
-
additional information
?
-
Plasmodium falciparum Tanzania (20000708)
substrate molecular docking study, binding site mapping and analysis
-
-
-
additional information
?
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
additional information
?
-
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
additional information
?
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Bacillus subtilis DSM 23778
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in he mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Francisella tularensis subsp. novicida Utah 112
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Plasmodium falciparum Tanzania (20000708)
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
additional information
Mg2+
-
absolute requirement of divalent metal ions like Ni2+, Mn2+, Co2+, Ca2+, Cu2+ and Zn2+ for catalytic acitvity, maximum activity with Mg2+
additional information
-
Cu2+, Ni2+, Ca2+, Fe2+ or Zn2+ do not serve as cofactor
additional information
poor activity with Mn2+, no activity with Ca2+, Co2+, Cu2+, and Zn2+
additional information
-
poor activity with Mn2+, no activity with Ca2+, Co2+, Cu2+, and Zn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3S)-1-(2,3,4-trifluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dibromophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dichlorophenyl)-N,N-dimethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
about 5% inhibition at 0.001 mM
(1R,3S)-1-(2,4-dichlorophenyl)-N-ethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4,5-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-bromo-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-fluorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-chloro-4-hydroxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methylphenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-fluoro-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(3,4-dimethoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(3-chloropyridin-4-yl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-bromo-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-bromo-2-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(4-carboxy-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2,6-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-methoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chlorophenyl)-1-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-fluoro-2-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-methyl-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[(2,4-dichlorophenyl)methyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-bis(dimethoxymethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-bis(trifluoromethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-MMV008138
(1R,3S)-MMV008138 targets the enzyme 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) in the MEP pathway. The Malaria Box compound MMV008138 targets the apicoplast and that parasite growth inhibition by this compound can be reversed by supplementation of IPP. The compound inhibits Plasmodium falciparum Dd2 strain growth with an IC50 value of 250 nM
-
(1S,3S)-1-(5-chlorothiophen-2-yl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole
about 7% inhibition at 0.001 mM
1-[(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-3-yl]-2-hydroxyethan-1-one
-
7-hydroxy-[1,2,4] triazolo[1,5-a] pyrimidine
azolopyrimidine, docking reveals strong hydrogen bonds with CTP-specific (T326, K406, R431, and K548) and MEP-specific (D428, R431, T525, and K548) amino acid residues of PvIspD protein. A salt-bridge formation is also observed with K406 and D428 residues similar to CTP
-
quercetin
quercetin is retained as a lead molecule for inhibition of IspD, 96% inhibition at 0.1 mM
rifampicin
a prokaryotic transcription inhibitor, interaction with residues T326, R431, T525, and K548
rosuvastatin
RST, significantly interacts at the active site of the enzyme. Active-site residues Gly16, Arg83, Thr84, and Thy190 are potentially contributing to the protein-ligand interaction
tunicamycin
interaction with residues V323, T324, T326, D338, L381, L384, K406, and T491
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
MMV008138, PfIspD is the sole intracellular target of MMV008138, target-based resistance. IspD binding mode analysis, overview. 1R,3S-MMV008138 directly inhibits purified recombinant Plasmodium falciparum IspD (PfIspD), competitively with its CTP substrate. The metabolic effects of 1R,3S-MMV008138 are specific to MEP pathway inhibition, 1R,3S-MMV008138 inhibits malaria parasite growth as a consequence of MEP pathway inhibition. 1R,3S-MMV008138 is also active against Plasmodium vivax but not against bacterial IspD homologues
-
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
MMV008138, Plasmodium vivax IspD (PvIspD) is potently inhibited by 1R,3S-MMV008138. IspD binding mode analysis, overview
-
fosmidomycin
Fos, a well-known inhibitor of DXR/IspC enzyme. Strong interaction of Fos with PvIspD enzyme, where hydrogen bonds are observed between Fos and amino acid residues D428, R431, Q493, T523, D524, T525 and K548 of PvIspD enzyme. residues R431 and K548 which form the salt bridge with CTP are observed to form a bridge with the negatively charged phosphate group of Fos
MMV008138
weak inhibition of Plasmodium vivax IspD, the compound is a competitive inhibitor of PvIspD at lower concentrations of CTP, interaction with residues D428, T525, and K548
-
additional information
high-throughput screening to identify inhibitors of MEP cytidylyltransferase (IspD)
-
additional information
bench-scale high-throughput screening to identify inhibitors of MEP cytidylyltransferase (IspD) using purified, recombinant IspD, a commercially available 1280 compound molecular library, and a 150 sample, in-house prepared, natural product extract library. The enzyme activity is not affected by 0.01% Triton X-100, but inhibition is attenuated in the presence of Triton X-100 for all inhibitors, except 6-hydroxy-DL-DOPA
-
additional information
no inhibition of Mycobacetrium tuberculosis IspD by (2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate, MMV008138
-
additional information
inhibitor screening and enzyme-inhibitor molecular docking study using enzyme structure with bound CTP and Mg2+ (PDB ID 3Q7U). The attached CTP and Mg2+ ion are deleted from the structure, followed by refinement of the protein subunit. The crucial active site residues Gly16, Arg83, Thr84, and Thy190 play a vital role in the protein-ligand stabilization process
-
additional information
the PfISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
additional information
-
the PfISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
additional information
inhibitor design and inhibition structure-activity relationships analysis, overview. In addition to (1R,3S)-configuration, potent growth inhibition requires 2',4'-disubstitution of the D-ring, featuring at least one electron-withdrawing substituent. Neither (1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (bearing an unsubstituted phenyl ring) nor (1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (bearing 2',4'-dimethyl substitution) inhibit Plasmodium falciparum growth at 0.01 mM. The 2'-chloro substituted analogue (1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid shows weak growth inhibition, and (1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (2'-chloro-4'-methyl substituted) nearly recapitulates the potency of (1R,3S)-MMV008138. The carboxy substituent at C3 of the C-ring also proves to be essential, replacement with CO2Me (3a) or H (11a) abrogates growth inhibition potency. But weak growth inhibition is restored with the first amide analogue (1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide, and methyl amide derivative (1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide proves equipotent to (1R,3S)-MMV008138. Not inhibitory: (1R,3S)-1-(3,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid, methyl (1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate.
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Effects of hypoxia, glucose deprivation and acidosis on phosphatidylcholine synthesis in HL-1 cardiomyocytes. CTP:phosphocholine cytidylyltransferase activity correlates with sarcolemmal disruption.
Carcinoma
[Primary analysis on protein maps of Helicobacter pylori strains associated with gastric carcinoma]
Herpes Simplex
Role of phosphatidyl-ethanolamine biosynthesis in herpes simplex virus 1 infected cells on progeny virus morphogenesis in the cytoplasm and on viral pathogenicity in vivo.
Infections
Role of phosphatidyl-ethanolamine biosynthesis in herpes simplex virus 1 infected cells on progeny virus morphogenesis in the cytoplasm and on viral pathogenicity in vivo.
Lymphoma, B-Cell
MYC is a positive regulator of choline metabolism and impedes mitophagy-dependent necroptosis in diffuse large B-cell lymphoma.
Lymphoma, Large B-Cell, Diffuse
MYC is a positive regulator of choline metabolism and impedes mitophagy-dependent necroptosis in diffuse large B-cell lymphoma.
Malaria
Plasmodium IspD (2-C-Methyl-D-erythritol 4-Phosphate Cytidyltransferase), an Essential and Druggable Antimalarial Target.
Neoplasms
Phosphoethanolamine Accumulation Protects Cancer Cells under Glutamine Starvation through Downregulation of PCYT2.
Neuroblastoma
Colocalisation of CTP:choline phosphate cytidylyltransferase (CT) with F-actin accompanies increased phosphatidylcholine synthesis in differentiating neuroblastoma cells.
stearoyl-coa 9-desaturase deficiency
Stearoyl-CoA desaturase 1 deficiency increases CTP:choline cytidylyltransferase translocation into the membrane and enhances phosphatidylcholine synthesis in liver.
Tuberculosis
Biosynthesis of isoprenoids: characterization of a functionally active recombinant 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development.
Tuberculosis
Homology modeling of Mycobacterium tuberculosis 2C-methyl-D-erythritol-4-phosphate cytidylyltransferase, the third enzyme in the MEP pathway for isoprenoid biosynthesis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02513
2-C-methyl-D-erythritol 4-phosphate
pH 7.9, 37°C, recombinant enzyme
0.043
2-C-methyl-D-erythritol 4-phosphate
calculated affinity
0.1248
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
0.2915
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
0.31
2-C-methyl-D-erythritol 4-phosphate
R20K mutant enzyme, pH 6.5, 23°C
0.37
2-C-methyl-D-erythritol 4-phosphate
wild type enzyme, pH 6.5, 23°C
0.74
2-C-methyl-D-erythritol 4-phosphate
R19K mutant enzyme, pH 6.5, 23°C
2.98
2-C-methyl-D-erythritol 4-phosphate
R19A mutant enzyme, pH 6.5, 23°C
3
2-C-methyl-D-erythritol 4-phosphate
K27S mutant enzyme, pH 6.5, 23°C
3.28
2-C-methyl-D-erythritol 4-phosphate
R20A mutant enzyme, pH 6.5, 23°C
15.5
2-C-methyl-D-erythritol 4-phosphate
D106E mutant enzyme, pH 6.5, 23°C
49
2-C-methyl-D-erythritol 4-phosphate
T140V mutant enzyme, pH 6.5, 23°C
131.5
2-C-methyl-D-erythritol 4-phosphate
R109A mutant enzyme, pH 6.5, 23°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
2-C-methyl-D-erythritol 4-phosphate
R109A mutant enzyme, pH 6.5, 23°C
0.75
2-C-methyl-D-erythritol 4-phosphate
K27S mutant enzyme, pH 6.5, 23°C
0.9
2-C-methyl-D-erythritol 4-phosphate
D106E mutant enzyme, pH 6.5, 23°C
4
2-C-methyl-D-erythritol 4-phosphate
T140V mutant enzyme, pH 6.5, 23°C
21.4
2-C-methyl-D-erythritol 4-phosphate
R20K mutant enzyme, pH 6.5, 23°C
36.35
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
36.8
2-C-methyl-D-erythritol 4-phosphate
R19A mutant enzyme, pH 6.5, 23°C
38.45
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
47.2
2-C-methyl-D-erythritol 4-phosphate
R19K mutant enzyme, pH 6.5, 23°C
48.4
2-C-methyl-D-erythritol 4-phosphate
wild type enzyme, pH 6.5, 23°C
52.7
2-C-methyl-D-erythritol 4-phosphate
R20A mutant enzyme, pH 6.5, 23°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
131.9
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
291.3
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000084
(1R,3S)-1-(2,4-dibromophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000044
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2,4-dichlorophenyl)-N-ethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000057
(1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.00023
(1R,3S)-1-(2,4-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000031
(1R,3S)-1-(2-bromo-4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000031
(1R,3S)-1-(2-bromo-4-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.0001
(1R,3S)-1-(2-chloro-4-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00028
(1R,3S)-1-(2-chloro-4-fluorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000082
(1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00036
(1R,3S)-1-(2-chloro-4-methylphenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00013
(1R,3S)-1-(2-fluoro-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000034
(1R,3S)-1-(4-bromo-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000021
(1R,3S)-1-(4-bromo-2-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.00014
(1R,3S)-1-(4-chloro-2-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00026
(1R,3S)-1-(4-chloro-2-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00051
(1R,3S)-1-(4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00014
(1R,3S)-1-(4-fluoro-2-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-[2,4-bis(dimethoxymethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-[2,4-bis(trifluoromethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000047 - 0.00032
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
-
0.000047
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium falciparum
recombinant wild-type enzyme, pH 7.0, 37°C
-
0.0001
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium falciparum
recombinant IspD mutant L244I, pH 7.0, 37°C
-
0.00031
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium vivax
recombinant wild-type enzyme, pH 7.0, 37°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00335
-
assay with D-1-deoxyxylulose-5-phosphate or 2-C-methyl-D-erythritol-4-phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
8.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme gene ispD is fused to gene ispF to encode a bifunctional enzyme catalyzing synthesis of 4-diphosphocytidyl2-C-methyl D-erythritol and of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
transcription level of enzyme remains constant for at least one month
brenda
embryonic root, transcription level of enzyme remains constant for at least one month
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme is a member of the cytidylyltransferase family of enzymes that utilize cytidine 5'-triphosphate (CTP) to synthesize molecules that are typically precursors to membrane phospholipids
evolution
structure, function and mechanism of Plasmodium IspD homologs from their evolutionary imprints, e.g. Theileria annulata. Structure-based phylogeny for PlIspD homologues, constructed by using the maximum likelihood algorithm with the Dayhoff model structure and structure motifs prediction and characterization of PlIspD homologues, overview
evolution
Plasmodium falciparum Tanzania (20000708)
-
structure, function and mechanism of Plasmodium IspD homologs from their evolutionary imprints, e.g. Theileria annulata. Structure-based phylogeny for PlIspD homologues, constructed by using the maximum likelihood algorithm with the Dayhoff model structure and structure motifs prediction and characterization of PlIspD homologues, overview
-
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro. 1R,3S-MMV008138-treated parasites supplemented with 0.2 mM isopentenyl diphosphate (IPP) are viable, but 1R,3S-MMV008138 treatment of such IPP-rescued cells still results in a significant reduction in methylerythritol cyclic diphosphate (MEcPP) levels, the most distal MEP metabolite detected
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
metabolism
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
metabolism
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
metabolism
Francisella tularensis subsp. novicida Utah 112
-
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
-
physiological function
2C-methyl-D-erythritol-4-phosphate cytidylyltransferase is the third enzyme in the MEP pathway for isoprenoid biosynthesis
physiological function
enzyme is part of the MEP pathway of biosynthesis of isoprenoid precursors
physiological function
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
physiological function
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
physiological function
enzyme 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) acts in the MEP pathway and converts MEP and cytidine triphosphate (CTP) to cytidine diphosphate methylerythritol (CDP-ME) and diphosphate
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme MCT plays an influential role in isoprenoid biosynthesis
physiological function
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
physiological function
Bacillus subtilis DSM 23778
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
-
physiological function
-
2C-methyl-D-erythritol-4-phosphate cytidylyltransferase is the third enzyme in the MEP pathway for isoprenoid biosynthesis
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
additional information
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
additional information
-
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
additional information
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
additional information
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
additional information
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
additional information
the Pf ISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme
additional information
-
the Pf ISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme
additional information
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
-
additional information
-
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
-
additional information
Bacillus subtilis DSM 23778
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
-
additional information
-
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
-
additional information
-
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
-
Show AA Sequence and Transmembrane Helices (32772 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25472
-
x * 29000, SDS-PAGE, x * 25472 is predicted from sequence of c DNA
25700
26000
26110
29000
-
x * 29000, SDS-PAGE, x * 25472 is predicted from sequence of c DNA
26110
-
SDS-polyacrylamide gel electrophoresis and mass spectrometry
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
monomer
-
sedimentation velocity experiments, both wild-type and mutant D152A
additional information
dimer
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
dimer
-
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
-
dimer
Bacillus subtilis DSM 23778
-
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
-
dimer
-
each subunit contains a globular core domain with an alpha/beta sturcture and and one smaller subdomain
dimer
the beta-domains of the monomers are mainly responsible for the formation of the dimer
dimer
-
the beta-domains of the monomers are mainly responsible for the formation of the dimer
-
dimer
-
the beta-domains of the monomers are mainly responsible for the formation of the dimer
-
additional information
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
additional information
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
additional information
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
-
additional information
Bacillus subtilis DSM 23778
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
sequence contains a N-terminal chloroplast transit peptide of 88 amino acids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of recombinant enzyme, structure contains a cytidine monophosphate bound in the active site suggesting a mechanism for feedback regulation of enzyme activity
purified IspD and IspD complexed with CTP and Mg2+, hanging drop vapour diffusion method, for the apoenzyme, 8 mg/ml protein in 25 mM Tris-HCl, pH 8.0, and 0.1 M NaCl, is mixed with 0.1 M Tris (pH 8.5), 20% v/v PEG monomethyl ether 2000, for the complexed enzyme 8 mg/ml protein in 25 mM Tris-HCl, pH 8.0, and 0.1 M NaCl, is mixed with 0.2 M MgCl2, 0.1 M HEPES, pH 7.5, 25% v/v PEG 3350, 18°C, X-ray diffraction structure determination and analysis, molecular replacement using the monomer of IspD enzyme from Arabidopsis thaliana (AtIspD) (PDB ID 2yc3) as template
hanging drop vapor diffusion method
hanging-drop vapour-diffusion using paoyethylene glycol as precipitant, elongated tetragonal prismatic crystals of 0.1 * 0.1 * 0.5 mm, space group P41212
-
vapor diffusion method at 4°C in hanging drops, crystals belong to space group C2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K213S
-
effective turnover rate is ca. 0.4% of the rate of wild type, retains capacity to form product with significantly reduced efficiency
K27A
K27S
E688Q
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by MMV008138 as compared to the wild-type enzyme
L244I
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by MMV008138 as compared to the wild-type enzyme
additional information
K27A
-
amino acid plays an essential role in catalysis because the effective turnover rate is ca. 0.025% of the rate of wild type enzyme
K27S
-
amino acid plays an essential role in catalysis because the effective turnover rate is ca. 0.025% of the rate of wild type enzyme
additional information
-
mutants have been constructed that contain a defect in the pathway to convert 2-C-methyl-D-erythritol 4-phosphate in the unknown product, several genes are cloned to complement the defect of these blocked mutants
additional information
heterologous expression in Escherichia coli lacking corresponding enzyme activity rescues the mutant
additional information
-
heterologous expression in Escherichia coli lacking corresponding enzyme activity rescues the mutant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
-
native-like tertiary structure, shapes of protein similar at 25°C, 30°C, and 40°C
50 - 80
-
unstable at temperature above 50°C, estimated by circular dichroism at 25°C to 80°C (far-UV and near-UV spectra) and after 10 min equilibration, partly integer secondary structure, occurrence of thermally-induced unfolding correlated with catalytic activity loss
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 4°C, from bacterial lysate by Ni-NTA metal affinity chromatography (elution with 200 mM imidazole), dialysis, concentration by ultrafiltration, yield of 2.8 mg/l culture
-
metal-chelating Hitrap clumn preloaded with Ni2+, Q-Sepharose anion-exchange chromatography to remove previously added thrombin
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the His tag is removed by thrombin enzyme, and followed by anion exchange chromatography and gel filtration, to 99% homogeneity
recombinant GST-tagged enzyme from Escherichia coli strain DH5alpha by glutathione affinity chromatography, the GST tag is removed by Prescission Protease (PPase) enzyme, and followed by anion exchange chromatography and gel filtration, to 99% homogeneity
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21 Codon Plus (DE3)-RIL by metal affinity chromatography and ultrafiltration
recombinant His-tagged wild-enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Sepharose Q FF column, Phenyl Sepharose, Cibacron blue 3GA column, Red Sepharose CL-6B column, Source 15 Q column
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 Codon Plus (DE3)-RIL by metal affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21 Codon Plus (DE3)-RIL by metal affinity chromatography and ultrafiltration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from genomic DNA in pET28a for expression with N-terminal hexa-His tag in Escherichia coli BL21 (DE3) for 12 h at 16°C
-
gene ispD, located on chromosome 1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene ispD, recombinant expression od wild-type enzyme in Escherichia coli
gene ispD, recombinant expression of a synthetic gene encoding codon-optimized PvISPD (PVX_081425) with a truncated N-terminal apicoplast localization sequence in Escherichia coli
gene ispD, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ispD, recombinant expression of GST-tagged enzyme in Escherichia coli strain DH5alpha
gene ispD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Codon Plus (DE3)-RIL
gene ispD, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene MCT, DNA and amino acid sequence determination and analysis, recombinant expression of GFP-tagged enzyme in Artemisia annua chloroplasts, recombinant overexpression in Arabidopsis thaliana leading to increases in chlorophyll a and b and carotinoid contents
gene PvispD, DNA and amino acid sequence determination and analysis, phylogenetic analysis of ispD proteins, recombinant expression of MBP-tagged PvIspD fusion protein in Escherichia coli strain ER2523 from plasmid pMALc2X-PvispD
into the vector pT7Blue for sequencing, a cDNA library is constructed in a PDONR222 vector
overexpression of several genes that could complement the defect of the mutants
-
gene ispD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Codon Plus (DE3)-RIL
gene ispD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Codon Plus (DE3)-RIL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
CTP:phosphocholine cytidylyltransferase enzyme assay that employs separation of non-radioactive 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from CTP. The assay can be applied to glycerol 3-phosphate cytidylyltransferase and CTP:2-C-methyl-D-erythritol-4-phosphate cytidylyltransferase synthetase (CMS), members of the cytidylyltransferase family that produce CDP-glycerol and CDP-methylerythritol, respectively
biotechnology
-
high-throughput methods for the screening of 2C-methyl-D-erythritol synthase IspC protein, 4-diphosphocytidyl-2C-methyl-D-erythritol synthase IspD protein, 4-diphosphocytidyl-2Cmethyl-D-erythritol kinase IspE protein, and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase IspF protein, against large compound libraries. Assays use up to three auxiliary enzymes monitored at 340 and all robust
drug development
medicine
drug development
-
due to the absence of the pathway in mammals enzyme provides a potential target for new antibiotics
drug development
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase, enzyme IspD, is a potential therapeutic drug target in Plasmodium vivax
drug development
IspD is a druggable target for the development of additional antimalarial agents. 1R,3S-MMV008138 shows promise as a potential scaffold for target-based antimalarial drug development
drug development
PfIspD enzyme inhibitor MMV008138 does not target the human IspD, reinforcing MMV008138 as a prototype of a distinct class of species-selective IspD-targeting antimalarial agents
drug development
the methyl erythritol phosphate (MEP) pathway, including enzyme MEP cytidylyltransferase (IspD), represents an attractive series of targets for antibiotic design, considering each enzyme of the pathway is both essential and has no human homologues
drug development
the methyl erythritol phosphate (MEP) pathway, including enzyme MEP cytidylyltransferase (IspD), represents an attractive series of targets for antibiotic design, considering each enzyme of the pathway is both essential and has no human homologues
drug development
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase, enzyme IspD, is a potential therapeutic drug target in Plasmodium vivax
-
drug development
Francisella tularensis subsp. novicida Utah 112
-
the methyl erythritol phosphate (MEP) pathway, including enzyme MEP cytidylyltransferase (IspD), represents an attractive series of targets for antibiotic design, considering each enzyme of the pathway is both essential and has no human homologues
-
medicine
the structure of CMS of Mycobacterium tuberculosis could be a starting point for structure-based design of new antituberculosis drugs
medicine
-
the structure of CMS of Mycobacterium tuberculosis could be a starting point for structure-based design of new antituberculosis drugs
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cane, D.E.; Chow, C.; Lillo, A.; Kang, I.
Molecular cloning, expression and characterization of the first three genes in the mevalonate-independent isoprenoid pathway in Streptomyces coelicolor
Bioorg. Med. Chem.
9
1467-1477
2001
Escherichia coli, Streptomyces coelicolor, Streptomyces coelicolor CH999
brenda
Richard, S.B.; Bowman, M.E.; Kwiatkowski, W.; Kang, L.; Chow, C.; Lillo, A.M.; Cane, D.E.; Noel, J.P.
Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis
Nature Struct. Biol.
8
641-648
2001
Escherichia coli, Mycobacterium tuberculosis, Plasmodium falciparum
brenda
Kemp, L.E.; Bond, C.S.; Hunter, W.N.
Crystallization and preliminary x-ray diffraction studies of recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase
Acta Crystallogr. Sect. D
57
1189-1191
2001
Escherichia coli
brenda
Rohdich, F.; Wungsintaweekul, J.; Eisenreich, W.; Richter, G.; Schuhr, C.A.; Hecht, S.; Zenk, M.H.; Bacher, A.
Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
97
6451-6456
2000
Arabidopsis thaliana, Escherichia coli (Q46893), Escherichia coli
brenda
Kuzuyama, T.; Takagi, M.; Kaneda, K.; Dairi, T.; Seto, H.
Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway
Tetrahedron Lett.
41
703-706
2000
Escherichia coli
-
brenda
Rohdich, F.; Wungsintaweekul, J.; Fellermeier, M.; Sagner, S.; Herz, S.; Kis, K.; Eisenreich, W.; Bacher, A.; Zenk, M.H.
Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol
Proc. Natl. Acad. Sci. USA
96
11758-11763
1999
Arabidopsis thaliana, Escherichia coli, Escherichia coli DH5-alpha
brenda
Gabrielsen, M.; Bond, C.S.; Hallyburton, I.; Hecht, S.; Bacher, A.; Eisenreich, W.; Rohdich, F.; Hunter, W.N.
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis
J. Biol. Chem.
279
52753-52761
2004
Agrobacterium tumefaciens, Campylobacter jejuni, Escherichia coli (Q46893), Escherichia coli
brenda
Kemp, L.E.; Bond, C.S.; Hunter, W.N.
Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Acta Crystallogr. Sect. D
59
607-610
2003
Escherichia coli
brenda
Bernal, C.; Palacin, C.; Boronat, A.; Imperial, S.
A colorimetric assay for the determination of 4-diphosphocytidyl-2-C-methyl-D-erythritol 4-phosphate synthase activity
Anal. Biochem.
337
55-61
2005
Escherichia coli
brenda
Richard, S.B.; Lillo, A.M.; Tetzlaff, C.N.; Bowman, M.E.; Noel, J.P.; Cane, D.E.
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and mutants, reveals roles of active site amino acids
Biochemistry
43
12189-12197
2004
Escherichia coli (Q46893), Escherichia coli
brenda
Zhao, X.; Miller, J.R.; Jiang, Y.; Marletta, M.A.; Cronan, J.E.
Assembly of the covalent linkage between lipoic acid and its cognate enzymes
Chem. Biol.
10
1293-1302
2003
Escherichia coli
brenda
Lherbet, C.; Pojer, F.; Richard, S.B.; Noel, J.P.; Poulter, C.D.
Absence of substrate channeling between active sites in the Agrobacterium tumefaciens IspDF and IspE enzymes of the methyl erythritol phosphate pathway
Biochemistry
45
3548-3553
2006
Agrobacterium tumefaciens
brenda
Gabrielsen, M.; Kaiser, J.; Rohdich, F.; Eisenreich, W.; Laupitz, R.; Bacher, A.; Bond, C.S.; Hunter, W.N.
The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate
FEBS J.
273
1065-1073
2006
Arabidopsis thaliana (P69834), Arabidopsis thaliana
brenda
Illarionova, V.; Kaiser, J.; Ostrozhenkova, E.; Bacher, A.; Fischer, M.; Eisenreich, W.; Rohdich, F.
Nonmevalonate terpene biosynthesis enzymes as antiinfective drug targets: substrate synthesis and high-throughput screening methods
J. Org. Chem.
71
8824-8834
2006
Escherichia coli
brenda
Kim, S.M.; Kuzuyama, T.; Chang, Y.J.; Kwon, H.J.; Kim, S.U.
Cloning and functional characterization of 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (GbMECT) gene from Ginkgo biloba
Phytochemistry
67
1435-1441
2006
Ginkgo biloba (Q0R5D7), Ginkgo biloba
brenda
Sando, T.; Takeno, S.; Watanabe, N.; Okumoto, H.; Kuzuyama, T.; Yamashita, A.; Hattori, M.; Ogasawara, N.; Fukusaki, E.; Kobayashi, A.
Cloning and characterization of the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway genes of a natural-rubber producing plant, Hevea brasiliensis
Biosci. Biotechnol. Biochem.
72
2903-2917
2008
Hevea brasiliensis (A9ZN09), Hevea brasiliensis (A9ZN10), Hevea brasiliensis
brenda
Shi, W.; Feng, J.; Zhang, M.; Lai, X.; Xu, S.; Zhang, X.; Wang, H.
Biosynthesis of isoprenoids: characterization of a functionally active recombinant 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) from Mycobacterium tuberculosis H37Rv
J. Biochem. Mol. Biol.
40
911-920
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Obiol-Pardo, C.; Cordero, A.; Rubio-Martinez, J.; Imperial, S.
Homology modeling of Mycobacterium tuberculosis 2C-methyl-D-erythritol-4-phosphate cytidylyltransferase, the third enzyme in the MEP pathway for isoprenoid biosynthesis
J. Mol. Model.
16
1061-1073
2010
Mycobacterium tuberculosis (P9WKG9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKG9)
brenda
Tsang, A.; Seidle, H.; Jawaid, S.; Zhou, W.; Smith, C.; Couch, R.
Francisella tularensis 2-C-Methyl-D-Erythritol 4-phosphate Cytidylyltransferase: Kinetic characterization and phosphoregulation
PLoS ONE
6
e20884
2011
Francisella tularensis, Francisella tularensis FSC155
brenda
Brault, J.P.; Friesen, J.A.
Characterization of cytidylyltransferase enzyme activity through high performance liquid chromatography
Anal. Biochem.
510
26-32
2016
Listeria monocytogenes
brenda
Imlay, L.; Armstrong, C.; Masters, M.; Li, T.; Price, K.; Edwards, R.; Mann, K.; Li, L.; Stallings, C.; Berry, N.; O'Neill, P.; Odom, A.
Plasmodium IspD (2-C-methyl-D-erythritol 4-phosphate cytidyltransferase), an essential and druggable antimalarial target
ACS Infect. Dis.
1
157-167
2016
Plasmodium vivax (A5K9U5), Mycobacterium tuberculosis (P9WKG9), Plasmodium falciparum (Q8I273), Plasmodium falciparum, Plasmodium vivax Salvador I (A5K9U5), Mycobacterium tuberculosis H37Rv (P9WKG9), Mycobacterium tuberculosis ATCC 25618 (P9WKG9)
brenda
Ghavami, M.; Merino, E.F.; Yao, Z.K.; Elahi, R.; Simpson, M.E.; Fernandez-Murga, M.L.; Butler, J.H.; Casasanta, M.A.; Krai, P.M.; Totrov, M.M.; Slade, D.J.; Carlier, P.R.; Cassera, M.B.
Biological studies and target engagement of the 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD)-targeting antimalarial agent (1 R,3 S)-MMV008138 and analogs
ACS Infect. Dis.
4
549-559
2018
Plasmodium falciparum (Q8I273)
brenda
Haymond, A.; Dowdy, T.; Johny, C.; Johnson, C.; Ball, H.; Dailey, A.; Schweibenz, B.; Villarroel, K.; Young, R.; Mantooth, C.J.; Patel, T.; Bases, J.; Dowd, C.S.; Couch, R.D.
A high-throughput screening campaign to identify inhibitors of DXP reductoisomerase (IspC) and MEP cytidylyltransferase (IspD)
Anal. Biochem.
542
63-75
2018
Francisella tularensis subsp. novicida (A0Q5K1), Escherichia coli (Q46893), Francisella tularensis subsp. novicida Utah 112 (A0Q5K1)
brenda
Saggu, G.S.; Garg, S.; Pala, Z.R.; Kochar, S.K.; Saxena, V.
Deciphering the role of IspD (2-C-methyl-D-erythritol 4-phosphate cytidyltransferase) enzyme as a potential therapeutic drug target against Plasmodium vivax
Gene
675
240-253
2018
Plasmodium vivax (A5K9U5), Plasmodium vivax, Plasmodium vivax Salvador I (A5K9U5)
brenda
Kumar, P.; Kumar, M.; Kumar, H.; Rana, S.; Kumar, J.; Sahoo, G.
In silico targeting methylerythritol phosphate pathway IspD enzyme of Mycobacterium tuberculosis for novel anti-mycobacterial drug discovery
J. Appl. Pharm. Sci.
10
23-29
2020
Mycobacterium tuberculosis (P9WKG9), Mycobacterium tuberculosis H37Rv (P9WKG9), Mycobacterium tuberculosis ATCC 25618 (P9WKG9)
-
brenda
Chellapandi, P.; Prathiviraj, R.; Prisilla, A.
Deciphering structure, function and mechanism of Plasmodium IspD homologs from their evolutionary imprints
J. Comput. Aided Mol. Des.
33
419-436
2019
Plasmodium falciparum (A0A024WEN0), Plasmodium falciparum Tanzania (20000708) (A0A024WEN0)
brenda
Jin, Y.; Liu, Z.; Li, Y.; Liu, W.; Tao, Y.; Wang, G.
A structural and functional study on the 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase (IspD) from Bacillus subtilis
Sci. Rep.
6
36379
2016
Bacillus subtilis (Q06755), Bacillus subtilis, Escherichia coli (Q46893), Escherichia coli, Bacillus subtilis 168 (Q06755), Bacillus subtilis DSM 23778 (Q06755)
brenda
Zhang, M.; Xiang, L.; Wang, H.; Lan, X.; Chen, M.; Liao, Z.
Molecular cloning and characterization of the 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase gene from Artemisia annua L
Yao Xue Xue Bao
51
1334-1339
2016
Artemisia annua (A0A1B2G2H8), Artemisia annua
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.7.60)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
