Dimethylallyltranstransferase

(Redirected from Farnesyl pyrophosphate synthase) Mammalian protein found in Homo sapiens

FDPS

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes

1YQ7, 1YV5, 1ZW5, 2F7M, 2F89, 2F8C, 2F8Z, 2F92, 2F94, 2F9K, 2OPM, 2OPN, 2QIS, 2RAH, 2VF6, 3B7L, 3CP6, 3N1V, 3N1W, 3N3L, 3N45, 3N46, 3N49, 3N5H, 3N5J, 3N6K, 3RYE, 3S4J, 4DEM, 4GA3, 4H5C, 4H5D, 4H5E, 4JVJ, 4KFA, 4KPD, 4KPJ, 4KQ5, 4KQS, 4KQU, 4L2X, 4LFV, 4LPG, 4LPH, 4N1Z, 4N9U, 4NFI, 4NFJ, 4NFK, 4NG6, 4NKE, 4NKF, 4NUA, 4OGU, 4P0V, 4P0W, 4P0X, 4PVX, 4PVY, 4Q23, 4QPF, 4QXS, 4RXA, 4XQR, 5CG5, 5DIQ, 5CG6, 5DJR, 5DJP, 4XQS, 5DJV, 5DGN, 4XQT, 5DGM, 5DGS

Identifiers

Aliases

FDPS, FPPS, FPS, POROK9, farnesyl diphosphate synthase

External IDs

OMIM: 134629; MGI: 104888; HomoloGene: 1519; GeneCards: FDPS; OMA:FDPS - orthologs

EC number

2.5.1.1

Gene location (Human)

Chr.	Chromosome 1 (human)

Band	1q22	Start	155,308,748 bp
Band	1q22	End	155,320,666 bp

Gene location (Mouse)

Chr.	Chromosome 3 (mouse)

Band	3 F1\|3 39.01 cM	Start	89,000,895 bp
Band	3 F1\|3 39.01 cM	End	89,009,266 bp

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ventricular zone

mucosa of transverse colon

ganglionic eminence

right adrenal gland

skin of thigh

tendon of biceps brachii

right adrenal cortex

right lobe of liver

upper lobe of left lung

mucosa of esophagus

Top expressed in

Mesencephalon

neural tube

morula

esophagus

hepatobiliary system

exocrine gland

liver

ovary

adrenal gland

More reference expression data

BioGPS

n/a

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

Orthologs

Species

Human

Mouse

Entrez


2224


110196

Ensembl


ENSG00000160752


ENSMUSG00000059743

UniProt


P14324


Q920E5

RefSeq (mRNA)

NM_001135821 NM_001135822 NM_001242824 NM_001242825 NM_002004
NM_001378424 NM_001378425


NM_001253751 NM_134469 NM_180985

RefSeq (protein)

NP_001129293 NP_001129294 NP_001229753 NP_001229754 NP_001995
NP_001365353 NP_001365354


NP_001240680 NP_608219

Location (UCSC)

Chr 1: 155.31 – 155.32 Mb

PubMed search

Dimethylallyltranstransferase

Identifiers

Databases

PDB structures

Search
PMC	articles
PubMed	articles
NCBI	proteins

Farnesyldiphosphate synthase (farnesylpyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)

Identifiers

Symbol

FDPS

Other data

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 enzyme that in humans is encoded by the FDPS gene and catalyzes the transformation of dimethylallylpyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP) into farnesylpyrophosphate (FPP).

Pyrophosphate is also involved, as both a reactant and a product. Geranylpyrophosphate is created in an intermediate step.

References

^ GRCh38: Ensembl release 89: ENSG00000160752 – Ensembl, May 2017
^ 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.
Banthorpe DV, Bucknall GA, Doonan HJ, Doonan S, Rowan MG (1976). "Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare". Phytochemistry. 15 (1): 91–100. Bibcode:1976PChem..15...91B. doi:10.1016/s0031-9422(00)89061-5.
Sagami H, Ogura K, Seto S, Kurokawa T (November 1978). "A new prenyltransferase from Micrococcus lysodeikticus". Biochemical and Biophysical Research Communications. 85 (2): 572–8. doi:10.1016/0006-291X(78)91201-9. 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.

Metabolism: lipid metabolism – ketones/cholesterol synthesis enzymes/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

Steroidogenesis

To pregnenolone

Cholesterol side-chain cleavage

To corticosteroids

aldosterone: 18-Hydroxylase

cortisol/cortisone: 17α-Hydroxylase
11β-HSD
- 1
- 2

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

v t e Transferases: alkyl and 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 t e 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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See also

References

External links