Dimethylallyltranstransferase

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Dimethylallyltranstransferase
Dimethylallyltranstransferase
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
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FDPS
Available structures
Gene ontology
Molecular function	transferase activity; metal ion binding; geranyltranstransferase activity; dimethylallyltranstransferase activity; RNA binding;
Cellular component	nucleoplasm; cytoplasm; cytosol; mitochondrion;
Biological process	cholesterol biosynthetic process; steroid metabolic process; viral process; cholesterol metabolic process; geranyl diphosphate biosynthetic process; sterol biosynthetic process; isoprenoid biosynthetic process; lipid metabolism; steroid biosynthetic process; farnesyl diphosphate biosynthetic process; regulation of cholesterol biosynthetic process;
	Sources:Amigo / QuickGO
	ENSG00000160752
	ENSMUSG00000059743
	P14324
	Q920E5
NM_001135821; NM_001135822; NM_001242824; NM_001242825; NM_002004;
	NM_001378424; NM_001378425
	NM_001253751; NM_134469; NM_180985
NP_001129293; NP_001129294; NP_001229753; NP_001229754; NP_001995;
	NP_001365353; NP_001365354
	NP_001240680; NP_608219
	Wikidata
View/Edit Human	View/Edit Mouse

Farnesyldiphosphate synthase (farnesylpyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)

Identifiers

Symbol

FDPS

Chr. 1 q22

Search for
Structures	Swiss-model
Domains	InterPro

Dimethylallyltranstransferase (DMATT), also known as farnesylpyrophosphate synthase (FPPS) or as farnesyldiphosphate synthase (FDPS), is an

farnesylpyrophosphate (FPP).^[5]^[6]

Geranylpyrophosphate

is created in an intermediate step.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000160752 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000059743 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
doi:10.1016/s0031-9422(00)89061-5
.

PMID 736921
.

External links

Dimethylallyltranstransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Overview of all the structural information available in the PDB for UniProt: P14324 (Human Farnesyl pyrophosphate synthaseC) at the PDBe-KB.

steroid metabolism
Mevalonate pathway
To HMG-CoA

Acetyl-Coenzyme A acetyltransferase

HMG-CoA synthase
(regulated step)

Ketogenesis

HMG-CoA lyase

3-hydroxybutyrate dehydrogenase

Thiophorase

To Mevalonic acid

HMG-CoA reductase

To DMAPP

Mevalonate kinase

Phosphomevalonate kinase

Pyrophosphomevalonate decarboxylase

Isopentenyl-diphosphate delta isomerase

Geranyl-

Dimethylallyltranstransferase

Geranyl pyrophosphate

To cholesterol
To lanosterol

Farnesyl-diphosphate farnesyltransferase

Squalene monooxygenase

Lanosterol synthase

7-Dehydrocholesterol path

Lanosterol 14α-demethylase

Sterol-C5-desaturase-like

7-Dehydrocholesterol reductase

Desmosterol path

24-Dehydrocholesterol reductase

To Bile acids

Cholesterol 7α-hydroxylase

Sterol 27-hydroxylase

Steroidogenesis
To pregnenolone

Cholesterol side-chain cleavage

To corticosteroids

aldosterone: 18-Hydroxylase

cortisol/cortisone: 17α-Hydroxylase

11β-HSD
1

2

both: 3β-HSD
1

2

21-Hydroxylase

11β-Hydroxylase

To sex hormones
To androgens

17α-Hydroxylase

17,20-Lyase

3β-HSD

17β-HSD

5α-Reductase

1

2

To estrogens

Aromatase

17β-HSD

Other/ungrouped

Steroid metabolism: sulfatase

Steroid sulfatase

sulfotransferase
SULT1A1

SULT2A1

Steroidogenic acute regulatory protein

Cholesterol total synthesis

Reverse cholesterol transport

aryl (EC 2.5)
2.5.1

Dimethylallyltranstransferase

Thiaminase I

Methionine adenosyltransferase

Riboflavin synthase

Dihydropteroate synthase

Spermidine synthase

Glutathione S-transferase

Farnesyl-diphosphate farnesyltransferase

Spermine synthase

Alkylglycerone phosphate synthase

Farnesyltransferase

Geranylgeranyltransferase type 1

Porphobilinogen deaminase

v
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Enzymes
Activity

Active site

Binding site

Catalytic triad

Oxyanion hole

Enzyme promiscuity

Diffusion-limited enzyme

Cofactor

Enzyme catalysis

Regulation

Allosteric regulation

Cooperativity

Enzyme inhibitor

Enzyme activator

Classification

EC number

Enzyme superfamily

Enzyme family

List of enzymes

Kinetics

Enzyme kinetics

Eadie–Hofstee diagram

Hanes–Woolf plot

Lineweaver–Burk plot

Michaelis–Menten kinetics

Types

EC1 Oxidoreductases (list)

EC2 Transferases (list)

EC3 Hydrolases (list)

EC4 Lyases (list)

EC5 Isomerases (list)

EC6 Ligases (list)

EC7 Translocases (list)

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v
t
e

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000160752 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000059743 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] :10.1016/s0031-9422(00)89061-5
.

[6] PMID 736921
.

[3]

[4]

[5]

[6]

See also

References

External links