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Search results 201 to 243 out of 243 for Ipp

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Type

Details

Score

Publication

23658024 | J:199658

First Author:	Moik D
Year:	2013
Journal:	J Biol Chem
Title:	Mutations in the paxillin-binding site of integrin-linked kinase (ILK) destabilize the pseudokinase domain and cause embryonic lethality in mice.
Volume:	288
Issue:	26
Pages:	18863-71

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Publication

25669897 | J:244756

First Author:	Morris EJ
Year:	2015
Journal:	Sci Rep
Title:	Integrin-linked kinase links dynactin-1/dynactin-2 with cortical integrin receptors to orient the mitotic spindle relative to the substratum.
Volume:	5

Pages:	8389

•

Publication

19153670 | -

First Author:	Fielding AB
Year:	2009
Journal:	Cancer Metastasis Rev
Title:	The mitotic functions of integrin-linked kinase.
Volume:	28
Issue:	1-2
Pages:	99-111

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Publication

16546570 | -

First Author:	Boulter E
Year:	2006
Journal:	Eur J Cell Biol
Title:	Integrin-linked kinase and its partners: a modular platform regulating cell-matrix adhesion dynamics and cytoskeletal organization.
Volume:	85
Issue:	3-4
Pages:	255-63

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Protein Domain

IPR035692 | PK_ILK

Type:

Domain

Description:

The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Integrin linked kinase (ILK) contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration []. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase []. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation [, ]. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin [, ].

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Publication

10841550 | -

First Author:	Rohdich F
Year:	2000
Journal:	Proc Natl Acad Sci U S A
Title:	Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana.
Volume:	97
Issue:	12
Pages:	6451-6

•

Publication

17081012 | -

First Author:	Illarionova V
Year:	2006
Journal:	J Org Chem
Title:	Nonmevalonate terpene biosynthesis enzymes as antiinfective drug targets: substrate synthesis and high-throughput screening methods.
Volume:	71
Issue:	23
Pages:	8824-34

•

Publication

17921290 | -

First Author:	Eoh H
Year:	2007
Journal:	J Bacteriol
Title:	Characterization of the Mycobacterium tuberculosis 4-diphosphocytidyl-2-C-methyl-D-erythritol synthase: potential for drug development.
Volume:	189
Issue:	24
Pages:	8922-7

•

Publication

24058607 | J:207543

First Author:	Donthamsetty S
Year:	2013
Journal:	PLoS One
Title:	Role of PINCH and its partner tumor suppressor Rsu-1 in regulating liver size and tumorigenesis.
Volume:	8
Issue:	9
Pages:	e74625

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Protein

H3BLP1

Organism:	Mus musculus/domesticus
Length:	146
Fragment?:	true

•

Protein

H3BKD7

Organism:	Mus musculus/domesticus
Length:	163
Fragment?:	true

•

Protein

H3BLF8

Organism:	Mus musculus/domesticus
Length:	163
Fragment?:	true

•

Protein

G3XA48

Organism:	Mus musculus/domesticus
Length:	283
Fragment?:	false

•

Publication

11004185 | -

First Author:	Cunningham FX Jr
Year:	2000
Journal:	J Bacteriol
Title:	Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid biosynthesis.
Volume:	182
Issue:	20
Pages:	5841-8

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Publication

11818558 | -

First Author:	Rohdich F
Year:	2002
Journal:	Proc Natl Acad Sci U S A
Title:	Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein.
Volume:	99
Issue:	3
Pages:	1158-63

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Publication

9537400 | -

First Author:	Potter S
Year:	1998
Journal:	J Bacteriol
Title:	Occurrence of homologs of the Escherichia coli lytB gene in gram-negative bacterial species.
Volume:	180
Issue:	7
Pages:	1959-61

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Publication

16289098 | -

First Author:	Röhrich RC
Year:	2005
Journal:	FEBS Lett
Title:	Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum.
Volume:	579
Issue:	28
Pages:	6433-8

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Publication

15863698 | -

First Author:	Hsieh MH
Year:	2005
Journal:	Plant Physiol
Title:	The Arabidopsis IspH homolog is involved in the plastid nonmevalonate pathway of isoprenoid biosynthesis.
Volume:	138
Issue:	2
Pages:	641-53

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Publication

19074383 | -

First Author:	Baur S
Year:	2009
Journal:	J Bacteriol
Title:	Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae.
Volume:	191
Issue:	4
Pages:	1200-10

•

Publication

26687144 | -

First Author:	Riemersma M
Year:	2015
Journal:	Chem Biol
Title:	Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation.
Volume:	22
Issue:	12
Pages:	1643-52

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Protein Domain

IPR034683 | IspD/TarI

Type:

Family

Description:

This family consists of cytidylyltransferases IspD and TarI.2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) in the deoxyxylulose pathway of isopentenyl diphosphate (IPP) biosynthesis []. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. The isoprenoid pathway is a well known target for anti-infective drug development [, ]. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein.Ribitol-5-phosphate cytidylyltransferase (TarI) is required for the synthesisof activated ribitol via the wall teichoic acid biosynthesis pathway. The enzyme catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate to form CDP-ribitol [].The human IspD (known as D-ribitol-5-phosphate cytidylyltransferase or isoprenoid synthase domain-containing protein) shows a canonical N-terminal cytidyltransferase domain linked to a C-terminal domain that is absent in cytidyltransferase homologues. It has cytidyltransferase activity toward pentose phosphates, including ribulose 5-phosphate, ribose 5-phosphate, and ribitol 5-phosphate. It is implicated in dystroglycan O-mannosylation [, ].

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Protein Domain

IPR017833 | Hopanoid_synth-assoc_rSAM_HpnH

Type:

Family

Description:

Proteins in this entry are members of the radical SAM superfamily of enzymes that utilise an iron-sulphur redox cluster and S-adenosylmethionine to carry out diverse radical mediated reactions []. This group of proteins are frequently encoded in the same locus as squalene-hopene cyclase (SHC, ) and other proteins associated with the biosynthesis of hopanoid natural products. The linkage between SHC and this radical SAM enzyme is strong; one is nearly always observed in the same genome where the other is found. A hopanoid biosynthesis locus was described in Zymomonas mobilis consisting of the genes for HpnA-E and SHC (HpnF) []. Continuing past SHC are the genes for a phosphorylase enzyme (ZMO0873, i.e. HpnG, ) and this radical SAM enzyme (ZMO0874) which we name here HpnH. Granted, in Z. mobilis, HpnH is in a convergent orientation with respect to HpnA-G, but one gene beyond HpnH and running in the same convergent direction is IspH (ZM0875, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase), an essential enzyme of IPP biosynthesis and therefore essential for the biosynthesis of hopanoids. One of the well-described hopanoid intermediates is bacteriohopanetetrol. In the conversion from hopene several reactions must occur in the side chain for which a radical mechanism might be reasonable. These include the four (presumably anaerobic) hydroxylations and a methyl shift.

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Protein Domain

IPR029765 | Mev_diP_decarb

Type:

Family

Description:

This group of enzymes belongs to the GHMP kinase domain superfamily. GHMP kinases are a unique class of ATP-dependent enzymes (the abbreviation of which refers to the original members: galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) []. Enzymes belonging to this superfamily contain three well-conserved motifs, the second of which has the typical sequence Pro-X-X-X-Gly-Leu-X-Ser-Ser-Ala and is involved in ATP binding []. The phosphate binding loop in GHMP kinases is distinct from the classical P-loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P-loop-containing proteins []. GHMP kinases display a distinctly bilobal appearance with their N-terminal subdomains dominated by a mixed β-sheet flanked on one side by α-helices and their C-terminal subdomains containing a four stranded anti-parallel β-sheet [, , , ]. Diphosphomevalonate decarboxylase (mevalonate pyrophosphate decarboxylase, () catalyzes the decarboxylation of mevalonate pyrophosphate to isopentyl pyrophosphate (IPP) [], the last step in the synthesis of IPP in the mevalonate pathway. In archaea, an alternate pathway involves decarboxylation of mevalonate monophosphate instead of diphosphomevalonate []. Mevalonate is a key intermediate in the biosynthesis of sterols and non-sterol isoprenes in the mevalonate pathway. In mammals, the majority of mevalonate is converted into cholesterol.ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2

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Protein Domain

IPR005935 | Mev_decarb

Type:

Family

Description:

This group of enzymes belongs to the GHMP kinase domain superfamily. GHMP kinases are a unique class of ATP-dependent enzymes (the abbreviation of which refers to the original members: galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) []. Enzymes belonging to this superfamily contain three well-conserved motifs, the second of which has the typical sequence Pro-X-X-X-Gly-Leu-X-Ser-Ser-Ala and is involved in ATP binding[]. The phosphate binding loop in GHMP kinases is distinct from the classical P-loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P-loop-containing proteins []. GHMP kinases display a distinctly bilobal appearance with their N-terminal subdomains dominated by a mixed β-sheet flanked on one side by α-helices and their C-terminal subdomains containing a four stranded anti-parallel β-sheet [, , , ]. Diphosphomevalonate decarboxylase (mevalonate pyrophosphate decarboxylase, () catalyzes the decarboxylation of mevalonate pyrophosphate to isopentyl pyrophosphate (IPP) [], the last step in the synthesis of IPP in the mevalonate pathway. In archaea, an alternate pathway involves decarboxylation of mevalonate monophosphate instead of diphosphomevalonate []. Mevalonate is a key intermediate in the biosynthesis of sterols and non-sterol isoprenes in the mevalonate pathway. In mammals, the majority of mevalonate is converted into cholesterol.ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2 The classical mevalonate (MVA) pathway involves decarboxylation of mevalonate diphosphate, while an alternate pathway involves decarboxylation of mevalonate monophosphate. The enzyme responsible is known as phosphomevalonate decarboxylase [].

•

Protein Domain

IPR003451 | LytB/IspH

Type:

Family

Description:

Terpenes are among the largest groups of natural products and include compounds such as vitamins, cholesterol and carotenoids. The biosynthesis of all terpenoids begins with one or both of the two C5 precursors of the pathway: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). In animals, fungi, and certain bacteria, the synthesis of IPP and DMAPP occurs via the well-known mevalonate pathway, however, a second, nonmevalonate terpenoid pathway has been identified in many eubacteria, algae, malaria parasite and the chloroplasts of higher plants [, , ].LytB(IspH) is the last enzyme in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the 1-deoxy-d-xylulose-5-phosphate (DOXP, the nonmevalonate pathway, also known as MEP) pathway []. This enzyme contains a [4Fe-4S]cluster and forms a stable complex with ferredoxin, which suggests that ferredoxin/ferredoxin-NADP+ reductase redox system serves as the physiological electron donor for LytB []. Escherichia coli LytB protein had been found to regulate the activity of RelA (guanosine 3',5'-bispyrophosphate synthetase I), which in turn controls the level of a regulatory metabolite. It is involved in penicillin tolerance and the stringent response [].

•

Publication

7947744 | -

First Author:	Dhe-Paganon S
Year:	1994
Journal:	Biochemistry
Title:	Mechanism of mevalonate pyrophosphate decarboxylase: evidence for a carbocationic transition state.
Volume:	33
Issue:	45
Pages:	13355-62

•

Publication

24375100 | -

First Author:	Vannice JC
Year:	2014
Journal:	J Bacteriol
Title:	Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway.
Volume:	196
Issue:	5
Pages:	1055-63

•

Publication

27194101 | J:239923

First Author:	Gerin I
Year:	2016
Journal:	Nat Commun
Title:	ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto α-dystroglycan.
Volume:	7

Pages:	11534

•

Protein

Q5RJG7

Organism:	Mus musculus/domesticus
Length:	447
Fragment?:	false

•

Protein

A0A1Y7VM96

Organism:	Mus musculus/domesticus
Length:	397
Fragment?:	false

•

Protein

A0A1Y7VK76

Organism:	Mus musculus/domesticus
Length:	348
Fragment?:	false

•

Publication

12135472 | -

First Author:	Liang PH
Year:	2002
Journal:	Eur J Biochem
Title:	Structure, mechanism and function of prenyltransferases.
Volume:	269
Issue:	14
Pages:	3339-54

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Protein

Q99JF5

Organism:	Mus musculus/domesticus
Length:	401
Fragment?:	false

•

Protein

Q3UYC1

Organism:	Mus musculus/domesticus
Length:	401
Fragment?:	false

•

Publication

12771135 | -

First Author:	Wada T
Year:	2003
Journal:	J Biol Chem
Title:	Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.
Volume:	278
Issue:	32
Pages:	30022-7

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Publication

12001237 | -

First Author:	Romanowski MJ
Year:	2002
Journal:	Proteins
Title:	Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily.
Volume:	47
Issue:	4
Pages:	568-71

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Publication

12796487 | -

First Author:	Thoden JB
Year:	2003
Journal:	J Biol Chem
Title:	Molecular structure of galactokinase.
Volume:	278
Issue:	35
Pages:	33305-11

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Publication

8382990 | -

First Author:	Bork P
Year:	1993
Journal:	Protein Sci
Title:	Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases.
Volume:	2
Issue:	1
Pages:	31-40

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Publication

11188689 | -

First Author:	Zhou T
Year:	2000
Journal:	Structure
Title:	Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.
Volume:	8
Issue:	12
Pages:	1247-57

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Protein

O55222

Organism:	Mus musculus/domesticus
Length:	452
Fragment?:	false

•

Publication

9714766 | -

First Author:	Perzl M
Year:	1998
Journal:	Biochim Biophys Acta
Title:	Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids.
Volume:	1393
Issue:	1
Pages:	108-18

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Publication

11222759 | -

First Author:	Sofia HJ
Year:	2001
Journal:	Nucleic Acids Res
Title:	Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.
Volume:	29
Issue:	5
Pages:	1097-106

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Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

•

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