Information on EC 2.5.1.31 - ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]:
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EC NUMBERCOMMENTARY
2.5.1.31-

RECOMMENDED NAMEGeneOntology No.
ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]GO:0008834

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		----
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		active site structure and catalytic mechanismEscherichia coli-659232
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		active site structure, detailed catalytic mechanism, substrate binding mechanism, D26, H43, S71, N74, and R77 are involved; active site structure, detailed catalytic mechanism, substrate binding mechanism, D26, H43, S71, N74, and R77 are involvedEscherichia coli-659476
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		ditrans,octacis-undecaprenyl diphosphate substrate binding mode and catalytic mechanism involving active site residue Asp26 which serves as general base, overview; substrate binding mode and catalytic mechanism involving active site residue Asp26 which serves as general base, overviewEscherichia coli-660464

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
alkenyl group transfer----

PATHWAYKEGG LinkMetaCyc Link
di-trans,poly-cis-undecaprenyl phosphate biosynthesis-PWY-5785

SYSTEMATIC NAMEIUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
bactoprenyl-diphosphate synthase----
C55-OO synthetase----
C55PP synthetase----
cis,polyprenyl diphosphate synthase----
cis-prenyl chain elongating enzymeMicrococcus luteus--637489
cis-type undecaprenyl pyrophosphate synthaseEscherichia coli--657857
CPDS----
DDPPs----
dehydrodolichyl diphosphate synthase----
di-trans,poly-cis-decaprenylcistransferaseEscherichia coli, Haemophilus influenzae--708911
di-trans,poly-cis-decaprenylcistransferaseHaemophilus influenzaeP44938-708911
di-trans,poly-cis-decaprenylcistransferaseStreptococcus pneumoniae R6--708911
synthetase, undecaprenyl pyrophosphate----
undecaprenyl diphosphate synthase----
undecaprenyl diphosphate synthaseMicrococcus luteus--637487, 637489, 637491, 637492, 673055, 685691, 706947
undecaprenyl diphosphate synthaseMicrococcus luteus-; 659084
undecaprenyl diphosphate synthaseEscherichia coli--673055
undecaprenyl diphosphate synthaseBacillus subtilis--708500
undecaprenyl diphosphate synthetase----
undecaprenyl pyrophosphate synthaseEscherichia coli--637485, 637494, 637495, 657857, 659232, 660464, 676880, 699031, 707467, 708864
undecaprenyl pyrophosphate synthaseEscherichia coli-; 659476
undecaprenyl pyrophosphate synthaseMicrococcus luteus--673574
undecaprenyl pyrophosphate synthaseHelicobacter pyloriP55984-699031
undecaprenyl pyrophosphate synthaseStreptococcus pneumoniae--707529
undecaprenyl pyrophosphate synthetase----
undecaprenyl pyrophosphate synthetaseBacillus subtilis--637474
undecaprenyl pyrophosphate synthetaseEscherichia coli--637482, 708911
undecaprenyl pyrophosphate synthetaseHaemophilus influenzaeP44938-708911
undecaprenyl pyrophosphate synthetaseStreptococcus pneumoniae R6--708911
undecaprenyl-diphosphate synthase----
undecaprenyl-pyrophosphate synthaseEscherichia coli--637493
UPP synthaseMicrococcus luteus--637492, 659084, 673055, 685691
UPP synthaseEscherichia coli--673055
UPP synthetase----
UPP synthetaseEscherichia coli--637482, 708911
UPP synthetaseHaemophilus influenzaeP44938-708911
UPP synthetaseStreptococcus pneumoniae R6--708911
UPP, C55 synthaseMicrococcus luteus--673574
UPPsEscherichia coli--637485, 637493, 637494, 637495, 657857, 659232, 660464, 699031, 704720, 707467, 708864
UPPsEscherichia coli-; 659476
UPPsHelicobacter pylori--699031, 704720
UPPsStreptococcus pneumoniae--707529
UPS----
UPSMicrococcus luteus--637489, 706947
Z-prenyl diphosphate synthase----
di-trans,poly-cis-undecaprenyl-diphosphate synthase----
additional informationEscherichia coli-cis-type enzyme657857, 660464
additional informationMicrococcus luteus-cis-type prenyl transferase659084

CAS REGISTRY NUMBERCOMMENTARY
52350-87-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus subtilis-637474, 637475, 708500--Manually annotated by BRENDA team
Escherichia coli-637479, 637482, 637485, 637488, 637493, 637494, 637495, 657857, 659232, 659476, 660464, 673055, 676880, 699031, 704720, 707467, 708864--Manually annotated by BRENDA team
Escherichia coli-637493, 659476, 699031P60472UniProtManually annotated by BRENDA team
Escherichia coliXL2-Blue and BL21(DE3)(pLysS)708911--Manually annotated by BRENDA team
Haemophilus influenzae-708911P44938UniprotManually annotated by BRENDA team
Helicobacter pylori-699031P55984UniProtManually annotated by BRENDA team
Helicobacter pylori-699031, 704720--Manually annotated by BRENDA team
Lactobacillus plantarum-637477, 637478, 637480, 637483, 637484--Manually annotated by BRENDA team
Lactobacillus plantarumATCC 8014637473Q88VJ8UniProtManually annotated by BRENDA team
Lactobacillus plantarumATCC 8014637473, 637475--Manually annotated by BRENDA team
Micrococcus luteus-637475, 637481--Manually annotated by BRENDA team
Micrococcus luteusB-P 26637476, 637489, 637492--Manually annotated by BRENDA team
Micrococcus luteusB-P 26637487, 637488, 637489, 637491, 637492, 659084, 706947O82827UniProtManually annotated by BRENDA team
Micrococcus luteusB-P 26; strain B-P 26685691--Manually annotated by BRENDA team
Micrococcus luteusstrain B-P 26659084--Manually annotated by BRENDA team
Micrococcus luteusstrain B-P 26673055, 673574O82827UniProtManually annotated by BRENDA team
Micrococcus luteus B-Pstrain B-P 26659084--Manually annotated by BRENDA team
Micrococcus luteus B-Pstrain B-P 26673055O82827-Manually annotated by BRENDA team
Micrococcus luteus B-P 26B-P 26637476--Manually annotated by BRENDA team
Micrococcus luteus B-P 26B-P 26637487O82827-Manually annotated by BRENDA team
Saccharomyces cerevisiae-637486--Manually annotated by BRENDA team
Salmonella newington-637475--Manually annotated by BRENDA team
Streptococcus pneumoniae-707529--Manually annotated by BRENDA team
Streptococcus pneumoniae R6-708911--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
(2E, 6E)-farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans,poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli--704720--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Bacillus subtilis--637475---
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Bacillus subtilis--637474, 708500--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli--637485, 637488, 637494, 637495, 657857, 659232, 660464, 707467, 708864--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Streptococcus pneumoniae--707529--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus--637475, 637481---
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus--637476--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteusO82827-637487--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus--637488, 637491, 685691--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coliP60472-637493--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli--659476, 699031--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Helicobacter pyloriP55984-699031--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus--637489, 637492, 659084--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli--637485quantification of product distribution of UPPs catalyzed coupling of (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate under various reaction conditions-?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Lactobacillus plantarumQ88VJ8trans,trans-farnesyl diphosphate637473C55 polyprenyl diphosphate with isoprene residues with cis stereochemistry-?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-catalyzes the cis-prenyl chain elongation onto trans,trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP). The product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls637489--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-catalyzes the condensation of eight molecules of isopentenyl pyrophosphate (IPP) with farnesyl diphosphate (FPP) to generate C55 undecaprenyl diphosphate. With a variety of different ratios of enzyme to substrate and FPP to IPP in the presence or absence of Triton, different product distributions are found637485--?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-catalyzes the sequential condensation of eight molecules of isopentenyl diphosphate (IPP) in the cis-configuration into farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of the bacterial cell wall659084--?
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphatediphosphate + ditrans,polycis-undecaprenyl diphosphate
show the reaction diagram		Helicobacter pylori--704720--?
(2E,6E)-farnesyl thiodiphosphate + isopentenyl diphosphate?
show the reaction diagram		Escherichia coli-weak activity, 10000000fold lower than with (2E,6E)-farnesyl diphosphate637494--?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474--?
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Micrococcus luteus--637492--?
(2Z,6E)-famesyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474--?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474, 708500--?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Micrococcus luteusO82827-637487--?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Micrococcus luteus--637491, 685691, 637492--?
(2Z,6E,10E,14E)-farnesylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474--?
(2Z,6Z,10E,14E)-farnesylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474--?
(E)-3-methyl-3-pentenyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis-reactive as substrate and competitive inhibition profile708500--?
7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one geranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Escherichia coli-fluorescent analogue of (2E,6E)-farnesyl diphosphate, alternative substrate and inhibitor708864--?
di-trans-poly-cis-decaprenyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-di-trans-poly-cis-decaprenyl diphosphate is farnesyl diphosphate659232--?
di-trans-poly-cis-decaprenyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-di-trans-poly-cis-decaprenyl diphosphate is farnesyl diphosphate, isopentenyl diphosphate binding mode determination659084--?
di-trans-poly-cis-decaprenyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-di-trans-poly-cis-decaprenyl diphosphate is farnesyl diphosphate, the diphosphate head group of farnesyl diphosphate is bound to the backbone of NHs pf G29 and R30 as well as the side chains of N28, R30, and R39 through hydrogen bonds, H43 may stabilize the farnesyl cation intermediate during catalysis being near to the C2 carbon of farnesyl diphosphate660464--?
farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-neither dimethylallyl diphosphate nor geranyl diphosphate act as priming substrate for the enzyme637482--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Helicobacter pyloriP55984-699031--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis659232, 659476--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis, the final product has C55 chain length660464--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis, the final product has C55-C60 chain length, molecular 3D-structural modeling of the reaction product657857--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-sequential condensation of 8 molecules of isopentenyl diphosphate in the cis-configuration into farnesyl diphosphate to produce undecaprenyl diphosphate, indispensable for the biosynthesis of bacterial cell wall659084--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-stereochemistry of the reaction659476--?
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-the phosphate head group of farnesyl diphosphate is bound to the positively charged Arg residues and the hydrocarbon moiety interacts with hydrophobic amino acids including L85, L88, and F89, located on the alpha3-helix of the enzyme657857--?
farnesyl phosphate + isopentenyl diphosphatephosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-low activity657857--?
geranyl diphosphate + isopentenyl diphosphatediphosphate + ?
show the reaction diagram		Escherichia coli-less effective than farnesyl diphosphate657857--?
geranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Escherichia coli-C10 GPP displays a 90fold larger Km value compared with (2E,6E)-farnesyl diphosphate 657857--?
geranylgeranyl diphosphate + isopentenyl diphosphatediphosphate + ?
show the reaction diagram		Escherichia coli-as effective as farnesyl diphosphate657857--?
geranylgeranyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Escherichia coli-containing a larger C20 hydrocarbon tail, is an equally good substrate657857--?
isopentenyl diphosphate + (E,E)-(2-diazo-3-trifluoropropionyloxy)geranyl diphosphate(E,E)-(2-diazo-3-trifluoropropionyloxy)polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--637479--?
isopentenyl diphosphate + (E,E)-(2-diazo-3-trifluoropropionyloxy)geranyl diphosphate(E,E)-(2-diazo-3-trifluoropropionyloxy)polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-47% of the activity with trans,trans-farnesyl diphosphate637478--?
isopentenyl diphosphate + DELTA3-isopentenyl diphosphate?
show the reaction diagram		Micrococcus luteus--637481--?
isopentenyl diphosphate + dimethylallyl diphosphate?
show the reaction diagram		Lactobacillus plantarum-2% of the activity with farnesyl diphosphate637480--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637478, 637484--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis--637475--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--637488-637488?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--637494, 637495, 673055, 676880--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--637476--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteusO82827-637487--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--637488-637488?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteusO82827-673055--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--673574--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Salmonella newington--637475--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Saccharomyces cerevisiae--637486the C55 polymer is the major product in presence of Triton X-100, without Triton C55-C75 polyprenyl diphosphates are generated637486?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coliP60472-637493the major product of the wild-type enzyme, and mutant enzymes H103A, V103A, V105A and I62A in presence of Triton is C55-polyprenyl diphosphate. Mutant enzyme L137A produces C55-polyprenyl diphosphate, C60-polyprenyl diphosphate and C65-polyprenyl diphosphate in the ration 55:41:4637493?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--637485product distribution under various reaction conditions. In the presence of excess farnesyl diphosphate the intermediates C25-C50 accumulate637485?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637477major products are undecaprenol and probably a longer chain polyprenol637477?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--637482with 0.02% Triton X-100 the main product is the C55-compound, C50-compound is the minor product. With 0.1% Triton X-100 the C50-polyprenyl diphosphate is the main product, the C55-polyprenyl diphosphate and the C45-polyprenyl diphosphate are minor products. With 0.5% Triton X-100 the C50-polyprenyl diphosphate compound and the C45-compound are the main products, the C55-compound is not formed637482?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-cis,trans-farnesyl diphosphate637481--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-cis,trans-farnesyl diphosphate637483C55-compound is formed as major product from trans,trans-farnesyl diphosphate, the C50-compound is formed as the major product from cis,trans-farnesyl diphosphate637483?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis-(E,E)-farnesyl diphosphate or (Z,E)-farnesyl diphosphate637474C50-polyprenyl diphosphate and C55-polyprenyl diphosphate in the ratio of 3:1 from (Z,E,E,E)-farnesylgeranyl diphosphate and in the ratio 3:2 from (Z,Z,E,E)-farnesylgeranyl diphosphate, C50-polyprenyl diphosphate and C55-polyprenyl diphosphate with Z,E mixed stereochemistry, formation of C50-polyprenyl diphosphate and C55-polyprenyl diphosphate in the ratio of 1:4 from (E,E)-farnesyl diphosphate and in the ratio of 4:1 from (Z,E)-farnesyl diphosphate637474?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-farnesyl diphosphate with mixed stereochemistry or trans,trans stereochemistry637480C55-polyprenyl diphosphate is the major product637480?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis-(Z,E,E,E)-farnesylgeranyl diphosphate or (Z,Z,E,E)-farnesylgeranyl diphosphate637474C50-polyprenyl diphosphate and C55-polyprenyl diphosphate in the ratio of 3:1 from (Z,E,E,E)-farnesylgeranyl diphosphate and in the ratio 3:2 from (Z,Z,E,E)-farnesylgeranyl diphosphate, C50-polyprenyl diphosphate and C55-polyprenyl diphosphate with Z,E mixed stereochemistry, formation of C50-polyprenyl diphosphate and C55-polyprenyl diphosphate in the ratio of 1:4 from (E,E)-farnesyl diphosphate and in the ratio of 4:1 from (Z,E)-farnesyl diphosphate637474?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-(E,E)-farnesyl diphosphate637492--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-trans,trans-farnesyl diphosphate and cis,trans-farnesyl diphosphate637475--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-(Z,E,E)-farnesyl diphosphate637491E193Q, R197S, E201Q, R203S, D221A, and D226A show product distribution pattern similar to that of the wild-type enzyme, which produces C55 prenyl diphosphate as its major product as well as minor amounts of some intermediates having shorter prenyl chains and C60 product. The major products of the mutant enzymes S74A and E216Q contain C35 and C50 prenyl chain length. Mutant enzyme F73A produces a mixture of C30 and C35 products637491?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-trans,trans-farnesyl diphosphate637475--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli-trans,trans-farnesyl diphosphate637479--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-trans,trans-farnesyl diphosphate637475, 637481, 637489--?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarumQ88VJ8trans,trans-farnesyl diphosphate637473C55 polyprenyl diphosphate with isoprene residues with cis stereochemistry637473?
isopentenyl diphosphate + farnesyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-trans,trans-farnesyl diphosphate637483C55-compound is formed as major product from trans,trans-farnesyl diphosphate, the C50-compound is formed as the major product from cis,trans-farnesyl diphosphate637483?
isopentenyl diphosphate + geranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637475--?
isopentenyl diphosphate + geranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis--637474, 637475--?
isopentenyl diphosphate + geranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--637475, 637481--?
isopentenyl diphosphate + geranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637483the C50-compound is the major product637483?
isopentenyl diphosphate + geranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-about 20% of the activity with farnesyl diphosphate637480C55-polyprenyl diphosphate is the major product637480?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637480--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis--637475--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Escherichia coli--673055--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--637475--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteusO82827-637487--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteusO82827-673055--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-(Z,E,E)-geranylgeranyl diphosphate637491, 637492--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus-trans,trans,trans-geranylgeranyl diphosphate and cis,trans,trans-geranylgeranyl diphosphate637481--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-trans,trans,trans-geranylgeranyl diphosphate and cis,trans,trans-geranylgeranyl diphosphate637483the C55-compound is formed as major product637483?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum-trans,trans,trans-geranylgeranyl diphosphate637475--?
isopentenyl diphosphate + geranylgeranyl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis-(E,E,E)-geranylgeranyl diphosphate or (Z,E,E)-geranylgeranyl diphosphate637474C50-prenyl diphosphate and C55-prenyl diphosphate in the ratio of 2:3 from (E,E,E)-geranyl diphosphate and in the ratio 1:3 from (Z,E,E)-geranylgeranyl diphosphate637474?
isopentenyl diphosphate + geranylneryl diphosphate?
show the reaction diagram		Lactobacillus plantarum-cis,trans,trans-geranylneryl diphosphate637475--?
isopentenyl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Escherichia coli--657857--?
isopentenyl diphosphate + neryl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum, Bacillus subtilis, Micrococcus luteus--637475--?
isopentenyl diphosphate + neryl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Micrococcus luteus--637481--?
isopentenyl diphosphate + neryl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Lactobacillus plantarum--637483the C50-compound is the major product637483?
isopentenyl diphosphate + neryl diphosphateC55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
show the reaction diagram		Bacillus subtilis--637474C45 prenyl diphosphate, C50 prenyl diphosphate and C55 prenyl diphosphate in the ratio of 2:10:1637474?
N-(4-benzoylphenyl)-4-hydroxy-2-oxo-5-phenethyl-2,5-dihydro-1H-pyrrole-3-carboxamide + isopentenyl diphosphate?
show the reaction diagram		Streptococcus pneumoniae-Photo-probe707529--?
neryl diphosphate + isopentenyl diphosphate?
show the reaction diagram		Bacillus subtilis--637474--?
isopentenyl diphosphate + S-farnesyl thiodiphosphate?
show the reaction diagram		Escherichia coli-weak activity, 10000000fold lower than with farnesyl diphosphate637494--?
additional information?-Micrococcus luteus-reactivities of the allylic substrates increase with chain length: C10, C15, C20. Each new isoprene unit added has a cis-configuration637481---
additional information?-Saccharomyces cerevisiae-the synthesized long-chain dehydrodolichyl diphosphate serves as a precursor of glycosyl carrier in glycoprotein biosynthesis in eukaryotes637486---
additional information?-Micrococcus luteus-the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls637489---
additional information?-Lactobacillus plantarum, Bacillus subtilis, Micrococcus luteus-involved in the biosynthesis of long-chain polyprenyl diphosphate required as a carbohydrate carrier in the biosynthesis of a variety of bacterial cell envelope components637475---
additional information?-Escherichia coli-role of the hydrocarbon moiety of the allylic substrate in the reaction657857---
additional information?-Micrococcus luteus-artificial substrate analogs, 3-desmethyl farnesyl diphosphate and 3-desmethyl Z-geranylgeranyl diphosphate are not used as substrates. The methyl group at the 3-position of the allylic substrate is important in the undecaprenyl diphosphate synthase reaction. The binding sites for the natural substrate farnesyl diphosphate and those for the intermediate allylic diphosphate, which contains the cis-prenyl unit, are different during the cis-prenyl chain elongation reaction685691---
additional information?-Escherichia coli-catalyzes the consecutive condensation reactions of a farnesyl diphosphate (FPP) with eight isopentenyl diphosphates (IPP), in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall659476---
additional information?-Micrococcus luteus-catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate637492---
additional information?-Bacillus subtilis-kinetic experiments with artificial substrate homologues708500---
additional information?-Micrococcus luteus-artificial substrate analogs, 3-desmethyl farnesyl diphosphate and 3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphate are not used as substrates. The methyl group at the 3-position of the allylic substrate is important in the undecaprenyl diphosphate synthase reaction. The binding sites for the natural substrate farnesyl diphosphate and those for the intermediate allylic diphosphate, which contains the cis-prenyl unit, are different during the cis-prenyl chain elongation reaction685691---
additional information?-Bacillus subtilis-Z-isomer ZHIPP, (Z)-3-methyl-3-pentenyl diphosphate, which is not accepted as substrate by the enzyme, exhibits no inhibition on the synthase reaction708500---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-catalyzes the cis-prenyl chain elongation onto trans,trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP). The product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls637489--
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-catalyzes the condensation of eight molecules of isopentenyl pyrophosphate (IPP) with farnesyl diphosphate (FPP) to generate C55 undecaprenyl diphosphate. With a variety of different ratios of enzyme to substrate and FPP to IPP in the presence or absence of Triton, different product distributions are found637485--
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-catalyzes the sequential condensation of eight molecules of isopentenyl diphosphate (IPP) in the cis-configuration into farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of the bacterial cell wall659084--
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis659232, 659476--
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis, the final product has C55 chain length660464--
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Escherichia coli-consecutive condensation of 8 molecules of isopentenyl diphosphate with farnesyl diphosphate to form the lipid carrier undecaprenyl diphosphate to mediate bacterial peptidoglycan synthesis, the final product has C55-C60 chain length, molecular 3D-structural modeling of the reaction product657857--
farnesyl diphosphate + isopentenyl diphosphatediphosphate + di-trans-poly-cis-undecaprenyl diphosphate
show the reaction diagram		Micrococcus luteus-sequential condensation of 8 molecules of isopentenyl diphosphate in the cis-configuration into farnesyl diphosphate to produce undecaprenyl diphosphate, indispensable for the biosynthesis of bacterial cell wall659084--
additional information?-Saccharomyces cerevisiae-the synthesized long-chain dehydrodolichyl diphosphate serves as a precursor of glycosyl carrier in glycoprotein biosynthesis in eukaryotes637486--
additional information?-Micrococcus luteus-the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls637489--
additional information?-Lactobacillus plantarum, Bacillus subtilis, Micrococcus luteus-involved in the biosynthesis of long-chain polyprenyl diphosphate required as a carbohydrate carrier in the biosynthesis of a variety of bacterial cell envelope components637475--
additional information?-Escherichia coli-catalyzes the consecutive condensation reactions of a farnesyl diphosphate (FPP) with eight isopentenyl diphosphates (IPP), in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall659476--
additional information?-Micrococcus luteus-catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate637492--
additional information?-Bacillus subtilis-kinetic experiments with artificial substrate homologues708500--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Micrococcus luteus-weak stimulation637491
Co2+Bacillus subtilis-divalent cation required637475
Co2+Lactobacillus plantarum-divalent cation required; enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+637475
Co2+Micrococcus luteus-divalent cation required; enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+637475
Co2+Lactobacillus plantarum-maximal stimulation at 0.1-0.3 mM637480
Co2+Micrococcus luteus-enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+637481
Co2+Micrococcus luteus-weak stimulation637491
K+Lactobacillus plantarumQ88VJ8stimulates in presence of Mg2+; stimulates in presence of Mg2+637473
K+Bacillus subtilis-stimulates in presence of Mg2+637474, 637475
K+Lactobacillus plantarum-stimulates in presence of Mg2+637475
KClEscherichia coli-activates at 50 mM659232
Mg2+Lactobacillus plantarumQ88VJ8required; required637473
Mg2+Bacillus subtilis-divalent cation required; optimal activity at 5 mM, required637474
Mg2+Bacillus subtilis-best stimulation by Mg2+. Mn2+ and Zn2+ may partially replace Mn2+; divalent cation required637475
Mg2+Lactobacillus plantarum-divalent cation required; enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+637475
Mg2+Micrococcus luteus-divalent cation required; enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+637475
Mg2+Lactobacillus plantarum-maximal stimulation at 0.1-0.3 mM637480
Mg2+Micrococcus luteus-maximal stimulation at 0.1 mM637481
Mg2+Escherichia coli-Mg2+ or Mn2+ required. Optimal concentration for Mg2+ is 1.0 mM; or Mn2+ required. Optimal concentration 1.0 mM637482
Mg2+Escherichia coli-dependend on637485
Mg2+Micrococcus luteus-divalent metal ion required, Mg2+ is most effective, optimal concentration is 240 nM637491
Mg2+Escherichia coli--657857
Mg2+Micrococcus luteus--659084
Mg2+Escherichia coli-is chelated by His199 and Glu213 from different subunits and possibly plays astructural rather than catalytic role; required, best at 0.5 mM MgCl2, 2 Mg2+ are bound at the subunit interface, binding structure659232
Mg2+Escherichia coli-role of the metal ion in catalysis, required for binding of isopentenyl diphosphate to the enzyme, best at 1 mM, low activity at 50 mM, Asp26 is required for efficient binding, Mg2+ is bound to the diphosphate of farnesyl diphosphate in the wild-type enzyme, but to the diphosphate of isopentenyl diphosphate in the mutant D26A, Mg2+ is not required for the overall structure stability, overview; role of the metal ion in catalysis, required for binding of isopentenyl diphosphate to the enzyme, best at 1 mM, low activity at 50 mM, Asp26 is required for efficient binding, Mg2+ is bound to the diphosphate of farnesyl diphosphate in the wild-type enzyme, but to the diphosphate of isopentenyl diphosphate in the mutant D26A, Mg2+ is not required for the overall structure stability, overview659476
Mg2+Escherichia coli-required, enzyme utilizes a Asp-rich motif for substrate binding via Mg2+660464
Mg2+Streptococcus pneumoniae--707529
Mg2+Escherichia coli-optimal concentration between 0.5 and 2 mM, dependend on708911
Mn2+Lactobacillus plantarumQ88VJ8; 637473
Mn2+Bacillus subtilis-can partially replace Mg2+; can partially replace Mg2+, optimal activity at 0.5 mM637474
Mn2+Micrococcus luteus-enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+637475, 637481
Mn2+Bacillus subtilis-best stimulation by Mg2+. Mn2+ and Zn2+ may partially replace Mn2+; can partially replace Mg2+637475
Mn2+Lactobacillus plantarum-enzyme is equally stimulated by 0.2 mM Mg2+, 0.2 mM Co2+ or 0.1 mM Mn2+637475
Mn2+Lactobacillus plantarum-effective in stimulation at 0.05-0.1 mM637480
Mn2+Escherichia coli-maximal stimulation at 0.05-0.1 mM, Mg2+ or Mn2+ required; Mn2+ or Mg2+ required; or Mg2+ required637482
Mn2+Micrococcus luteus-weak stimulation637491
Na+Lactobacillus plantarumQ88VJ8stimulates in presence of Mg2+; stimulates in presence of Mg2+637473
Na+Bacillus subtilis-stimulates in presence of Mg2+637474, 637475
Na+Lactobacillus plantarum-stimulates in presence of Mg2+637475
NH4+Lactobacillus plantarumQ88VJ8stimulates in presence of Mg2+; stimulates in presence of Mg2+637473
NH4+Bacillus subtilis-stimulates in presence of Mg2+637474, 637475
NH4+Lactobacillus plantarum-stimulates in presence of Mg2+637475
sulfateEscherichia coli-2 molecules bound per enzyme dimer, 1 at each active site, binding structure659232
TritonEscherichia coli-3 Triton (T1, T2, and T3) are located in the two monomers with one on the top portion of the active site tunnel in monomer A and the other two occupying the overall tunnel of monomer B707467
Zn2+Bacillus subtilis-can partially replace Mg2+637474, 637475
Zn2+Lactobacillus plantarum, Micrococcus luteus--637475
Zn2+Lactobacillus plantarum-maximal stimulation at 0.1-0.3 mM637480
Zn2+Micrococcus luteus-optimal concentration for activation is about 240 nM637491

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(2E,6E)-farnesyl thiodiphosphateEscherichia coli-(2E,6E)-farnesyl diphosphate analogue637494-
(2E,6E)-farnesyl thiodiphosphateStreptococcus pneumoniae-substrate analogue707529-
(2E,6E,10E)-4-methylfarnesyl diphosphateBacillus subtilis-competitive inhibitor against (2Z,6E,10E)-geranylgeranyl diphosphate708500-
(2Z,6E,10E)-4-methyl-geranylgeranyl diphosphateBacillus subtilis-allylic substrate homologue, competitive inhibitor against the allylic primer. It also acts as a strong noncompetitive inhibitor against isopentenyl diphosphate708500-
(4aS,8aS)-4-hydroxy-2-oxo-1,2,4a,5,6,7,8,8a-octahydro[1,6]naphthyridine-3-carboxylic acid (4-piperidin-1-ylphenyl)amideStreptococcus pneumoniae--707529-
(E)-3-methyl-3-pentenyl diphosphateBacillus subtilis-reactive as substrate and competitive inhibition profile708500-
(E,E)-[1-3H]-(2-diazo-3-trifluoropropionyloxy)geranyl diphosphateEscherichia coli--708911-
(S)-farnesyl thiodiphosphateEscherichia coli-an extremely poor substrate for UPPs708864 2D-image
1,2-CyclohexanedioneLactobacillus plantarumQ88VJ8; 637473 2D-image
1,2-CyclohexanedioneLactobacillus plantarum--637475 2D-image
3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mixed inhibition with farnesyl diphosphate, competitive inhibition with reaction intermediate (2Z,6E,10E)-geranylgeranyl diphosphate685691-
3-desmethyl farnesyl diphosphateMicrococcus luteus-competitive with farnesyl diphosphate, mixed inhibition with reaction intermediate (2Z,6E,10E)-geranylgeranyl diphosphate; competitive with farnesyl diphosphate, mixed inhibition with reaction intermediate (Z,E,E)-geranylgeranyl diphosphate685691 2D-image
3-desmethyl Z-geranylgeranyl diphosphateMicrococcus luteus-mixed inhibition with farnesyl diphosphate, competitive inhibition with reaction intermediate (Z,E,E)-geranylgeranyl diphosphate685691 2D-image
3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideEscherichia coli-barely inhibits UPPS of Escherichia coli; i.e. HTS04781. contrary to Helicobacter pylori, HTS04781 is almost not inhibitory in Escherichia coli699031 2D-image
3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideHelicobacter pyloriP55984; i.e. HTS04781, crystallization data. The sulfonamide group forms H-bonds with Gly16 and Arg26 and the N atom in the tetracyclic ring is hydrogen bound to the main chain of Met12. Extensive hydrophobic interactions are found between the tetracyclic ring with the surrounding residues including Met12, His30, Gly33 and Val34699031 2D-image
3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideEscherichia coli-barely inhibits UPPS of Escherichia coli704720 2D-image
3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideHelicobacter pylori--704720 2D-image
5-benzyl-4-hydroxy-5-methyl-2-oxo-2,5-dihydro-1H-pyrrole-3-carboxylic acid (4-cyclohexylphenyl)amideStreptococcus pneumoniae--707529-
7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one geranyl diphosphateEscherichia coli-competitive inhibitor, substrate analogue prepared and utilized to study ligand interactions708864-
BPH-629Escherichia coli-potent inhibitor676880 2D-image
ButanedioneLactobacillus plantarumQ88VJ8; 637473 2D-image
ButanedioneLactobacillus plantarum--637475 2D-image
EDTALactobacillus plantarum--637477 2D-image
EDTAMicrococcus luteus--637491 2D-image
farnesyl thiodiphosphateEscherichia coli--659476 2D-image
iodoacetateLactobacillus plantarum--637475 2D-image
isopentyl thiodiphosphateStreptococcus pneumoniae-substrate analogue707529-
N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideEscherichia coli-; i.e. BTB06061699031 2D-image
N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideHelicobacter pyloriP55984; i.e. BTB06061, crystallization data. The sulfur atom in the thiazole ring of BTB06061 may form H-bonds with Asn15 and His30 while the SO2 group is hydrogen bound with Met12. The aromatic rings of BTB06061 form hydrophobic interactions with the surrounding hydrophobic residues, including Val34, Leu37, Ala56 and Tyr79699031 2D-image
N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideEscherichia coli-barely inhibits UPPS of Escherichia coli704720 2D-image
N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideHelicobacter pylori--704720 2D-image
NH4+Bacillus subtilis-20 mM, 20% inhibition637474 2D-image
PhenylglyoxalLactobacillus plantarumQ88VJ8; 637473 2D-image
PhenylglyoxalLactobacillus plantarum--637475 2D-image
S-farnesyl thiodiphosphateEscherichia coli--637494 2D-image
SO42-Micrococcus luteus-competitive inhibitor with respect to (2E,6E)-farnesyl diphosphate; competitive inhibitor with respect to farnesyl diphosphate637492 2D-image
Triton X-100Micrococcus luteus-marked decrease of activity when a small amount of detergent is added, activity gradually increases as further detergent is added, being fully restored when the concentration reaches 2%637476 2D-image
Triton X-100Lactobacillus plantarum-inhibition at concentration above 1%637480 2D-image
Mg2+Escherichia coli-inhibitory at high concentrations of e.g. 50 mM; inhibitory at high concentrations of e.g. 50 mM659476 2D-image
additional informationLactobacillus plantarum-no inhibition by phosphate637475, 637477-
additional informationEscherichia coli-farnesol (1 mM) lacking the diphosphate does not inhibit the UPPS reaction; no inhibition by farnesol657857-
additional informationHelicobacter pyloriP55984virtual screening of inhibitors from a library of 58635 compounds performed699031-
additional informationStreptococcus pneumoniae-tetramic acids are selective and potent inhibitors of UPPS707529-
additional informationBacillus subtilis-Z-isomer ZHIPP, (Z)-3-methyl-3-pentenyl diphosphate, which is not accepted as substrate by the enzyme, exhibited no inhibition on the synthase reaction708500-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
capric acidLactobacillus plantarum-enhancement factor: 0.04 in absence of Triton X-100, 1.0 in presence of 0.1% Triton X-100637484 2D-image
cardiolipinLactobacillus plantarum-Lactobacillus plantarum, Escherichia coli, and bovine cardiolipin. Good activator in absence of detergent637475 2D-image
cardiolipinMicrococcus luteus-weak stimulation637475 2D-image
cardiolipinMicrococcus luteus-marked effect in activating lipid-depleted enzyme637476 2D-image
cardiolipinMicrococcus luteus-poor activator637481 2D-image
cardiolipinLactobacillus plantarum-activates637483 2D-image
cardiolipinLactobacillus plantarum-from bovine, enhancement factor: 0.8 in absence of Triton X-100, 0.1 in presence of 0.1% Triton X-100637484 2D-image
cetyl sulfateLactobacillus plantarum-half-maximal activation at 0.04 mM637475 2D-image
cetyl sulfateLactobacillus plantarum-activates637484 2D-image
deoxycholateBacillus subtilis-weak stimulation637475 2D-image
deoxycholateLactobacillus plantarum-half-maximal activation at 0.33 mM637475 2D-image
deoxycholateMicrococcus luteus-weak stimulation637475 2D-image
deoxycholateLactobacillus plantarum-maximal stimulation at 0.2% v/v or 4.8 mM637480 2D-image
deoxycholateMicrococcus luteus-poor activator637481 2D-image
deoxycholateLactobacillus plantarum-activates637484 2D-image
dipalmitoylphosphatidic acidLactobacillus plantarum-enhancement factor: 0.2 in absence of Triton X-100, 1.2 in presence of 0.1% Triton X-100637484 2D-image
Dodecyl sulfateLactobacillus plantarum-half-maximal activation at 0.075 mM637475 2D-image
Dodecyl sulfateLactobacillus plantarum-activates637484 2D-image
lauric acidLactobacillus plantarum-enhancement factor: 0.1 in absence of Triton X-100, 2.3 in presence of 0.1% Triton X-100637484 2D-image
lecithinBacillus subtilis-weak stimulation637475 2D-image
lecithinMicrococcus luteus-from egg, stimulates637475 2D-image
lecithinMicrococcus luteus-14fold stimulation at 2 mM; from egg, stimulates637481 2D-image
myristic acidLactobacillus plantarum-activates637483 2D-image
myristic acidLactobacillus plantarum-activates; enhancement factor: 0.2 in absence of Triton X-100, 2.1 in presence of 0.1% Triton X-100637484 2D-image
oleic acidLactobacillus plantarum-good activator in absence of detergent637475 2D-image
oleic acidLactobacillus plantarum-enhancement factor: 0.9 in absence of Triton X-100, 1.3 in presence of 0.1% Triton X-100637484 2D-image
palmitic acidLactobacillus plantarum-enhancement factor: 0.8 in absence of Triton X-100, 1.4 in presence of 0.1% Triton X-100637484 2D-image
phosphatidic acidLactobacillus plantarum-from egg, good activator in absence of detergent637475 2D-image
phosphatidic acidLactobacillus plantarum-enhancement factor: 0.8 in absence of Triton X-100, 1.0 in presence of 0.1% Triton X-100; from egg, good activator in absence of detergent637484 2D-image
phosphatidylglycerolMicrococcus luteus-marked effect in activating lipid-depleted enzyme637476 2D-image
phosphatidylserineLactobacillus plantarum-enhancement factor: 0.05 in absence of Triton X-100, 0.4 in presence of 0.1% Triton X-100637484 2D-image
PhospholipidMicrococcus luteus-phospholipid extract from Micrococcus luteus stimulates637481 2D-image
PhospholipidEscherichia coli--637485 2D-image
PolyaminesBacillus subtilis-stimulate in presence of Mg2+637474-
putrescineBacillus subtilis-stimulates637474 2D-image
stearic acidLactobacillus plantarum-enhancement factor: 0.07 in absence of Triton X-100, 0.8 in presence of 0.1% Triton X-100637484 2D-image
trans,trans,trans-geranylgeranyl diphosphateLactobacillus plantarum-stimulates activity with farnesyl diphosphate as substrate637483 2D-image
trans,trans-farnesyl diphosphateLactobacillus plantarum-stimulates activity with farnesyl diphosphate as substrate637483 2D-image
TritonEscherichia coli-0.01 microM of UPPs with 5 microM of (2E,6E)-farnesyl diphosphate and 50 microM of isopentenyl diphosphate, 0.5 mM MgCl2, and 50 mM KCl in Hepes buffer (pH 7.5) is 190fold less active (0.013 s-1) for the IPP consumption in the absence of Triton; the UPPs steady-state kcat value in the presence of 0.1% Triton is 190fold larger than in the absence of Triton637485 2D-image
Triton X-100Bacillus subtilis--637474 2D-image
Triton X-100Micrococcus luteus-stimulates637475, 637481 2D-image
Triton X-100Bacillus subtilis-strong stimulation637475 2D-image
Triton X-100Lactobacillus plantarum-half-maximal activation at 3.4 mM637475 2D-image
Triton X-100Micrococcus luteus-marked decrease of activity when a small amount of detergent is added, activity gradually increases as further detergent is added, being fully restored when the concentration reaches 2%637476 2D-image
Triton X-100Lactobacillus plantarum-activates; requirement for Triton X-series detergents637477 2D-image
Triton X-100Lactobacillus plantarum-activates637480, 637483 2D-image
Triton X-100Escherichia coli-no activity in absence; no activity in the activation by Triton X-100 is almost saturated at a concentration of 0.02%637482 2D-image
Triton X-100Escherichia coli-1.5% v/v, 2 molecules are bound in the active site tunnel of the beta-subunit, binding structure659232 2D-image
Triton X-100Escherichia coli, Micrococcus luteus--673055 2D-image
Triton X-102Lactobacillus plantarum-stimulates637477-
Triton X-114Lactobacillus plantarum-stimulates637477 2D-image
Triton X-45Lactobacillus plantarum-stimulates637477-
Tween 80Bacillus subtilis-stimulates637474 2D-image
Tween 80Bacillus subtilis-strong stimulation637475 2D-image
lysophosphatidylglycerolMicrococcus luteus-weak effect in activating lipid-depleted enzyme637476 2D-image
additional informationMicrococcus luteus-enzyme is inactive in absence of added effectors637481-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00011-(2E, 6E)-farnesyl diphosphateHelicobacter pylori-wild-type704720 2D-image
0.00015-(2E, 6E)-farnesyl diphosphateHelicobacter pylori-mutant C234A704720 2D-image
0.00011-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984wild type, pH 7.5, temperature not specified in the publication699031 2D-image
0.00013-(2E,6E)-farnesyl diphosphateLactobacillus plantarumQ88VJ8pH 7.5, 35°C637473 2D-image
0.00015-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5, temperature not specified in the publication699031 2D-image
0.00017-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)5 mutant707467 2D-image
0.00028-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, H199A mutant659232 2D-image
0.00037-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 1 mM MgCl2659476 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637485 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E73A mutant; pH 7.5, 25°C, E81A mutant; pH 7.5, 25°C, N74A mutant; pH 7.5, 25°C, wild type637493 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W91F, pH 7.5, 25°C, wild-type enzyme, pH 7.5, 25°C637494 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzymes E73A, D150A and D218A, pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637495 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-wild type, 25°C, pH 7.5657857 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type659232 2D-image
0.0004-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)1 mutant; pH 7.5, 25°C, wild type707467 2D-image
0.00044-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 3 mM MgCl2659476 2D-image
0.00046-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26K mutant with 0.5 mM MgCl2659476 2D-image
0.0005-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W221F, pH 7.5, 25°C637494 2D-image
0.0005-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme D26A, pH 7.5, 25°C637495 2D-image
0.0005-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26A mutant659232 2D-image
0.0005-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAS72 mutant707467 2D-image
0.00055-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26R mutant with 0.5 mM MgCl2659476 2D-image
0.00066-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, H199A/E213A mutant659232 2D-image
0.00067-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26E mutant with 0.5 mM MgCl2659476 2D-image
0.0007-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W149F, pH 7.5, 25°C637494 2D-image
0.0007-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme E213A, pH 7.5, 25°C637495 2D-image
0.0007-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E213A mutant659232 2D-image
0.001-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S71A mutant637493 2D-image
0.001-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAS83 mutant707467 2D-image
0.0015-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, W210A mutant659084 2D-image
0.0015-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 0.05 mM MgCl2659476 2D-image
0.00157-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 50 mM MgCl2659476 2D-image
0.0016-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, R77A mutant637493 2D-image
0.0016-(2E,6E)-farnesyl diphosphateEscherichia coli-L85A mutant, 25°C, pH 7.5657857 2D-image
0.0018-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W75F, pH 7.5, 25°C637494 2D-image
0.0018-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAV82S83 mutant707467 2D-image
0.002-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W31F, pH 7.5, 25°C637494 2D-image
0.0021-(2E,6E)-farnesyl diphosphateEscherichia coli-L88A mutant, 25°C, pH 7.5657857 2D-image
0.0023-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C637492 2D-image
0.0026-(2E,6E)-farnesyl diphosphateEscherichia coli-F89A mutant, 25°C, pH 7.5657857 2D-image
0.0028-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, Y148F mutant659084 2D-image
0.003-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, H43A mutant659232 2D-image
0.0032-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, W75A mutant637493 2D-image
0.0033-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C637492 2D-image
0.0034-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W207F, pH 7.5, 25°C637494 2D-image
0.0036-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492 2D-image
0.0049-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C637492 2D-image
0.005-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C637492 2D-image
0.0077-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, Y71S mutant659084 2D-image
0.0083-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637487 2D-image
0.0083-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, wild type659084 2D-image
0.0091-(2E,6E)-farnesyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.0092-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984wild type, pH 7.5, temperature not specified in the publication699031 2D-image
0.0096-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5, temperature not specified in the publication699031 2D-image
0.0104-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.0114-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C637492 2D-image
0.01213-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, W224A mutant659084 2D-image
0.0139-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.0147-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.0222-(2E,6E)-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, F207S mutant659084 2D-image
0.0231-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C637492 2D-image
0.0332-(2E,6E)-farnesyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C637492 2D-image
0.0495-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.1207-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
0.144-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492 2D-image
0.155-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N78D, pH 7.5, 37°C637487 2D-image
3.5-(2E,6E)-farnesyl diphosphateMicrococcus luteus-D221A mutant, pH 7.3, 37°C637491 2D-image
5.4-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E216Q mutant, pH 7.3, 37°C637491 2D-image
6.6-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E193Q mutant, pH 7.3, 37°C637491 2D-image
8.3-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild type, pH 7.3, 37°C637491 2D-image
9.2-(2E,6E)-farnesyl diphosphateMicrococcus luteus-F73A mutant, pH 7.3, 37°C637491 2D-image
9.6-(2E,6E)-farnesyl diphosphateMicrococcus luteus-S74A mutant, pH 7.3, 37°C637491 2D-image
11.2-(2E,6E)-farnesyl diphosphateMicrococcus luteus-D226A mutant, pH 7.3, 37°C637491 2D-image
11.6-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E201Q mutant, pH 7.3, 37°C637491 2D-image
13.6-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R203S mutant, pH 7.3, 37°C637491 2D-image
18-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R197S mutant, pH 7.3, 37°C637491 2D-image
0.0088-(2E,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492-
0.0093-(2E,6E,10E)-geranylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474-
0.064-(2E,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492-
0.0043-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C637492-
0.0045-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C637492-
0.005-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487-
0.005-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C637492-
0.0059-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R-R42G mutant, pH 7.5, 37°C637492-
0.006-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C637492-
0.0061-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C637492-
0.008-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C; mutant enzyme W78D, pH 7.5, 37°C637487-
0.0082-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487-
0.0082-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492-
0.0089-(2Z,6E,10E)-geranylgeranyl diphosphateBacillus subtilis-37°C, pH 37°C708500-
0.0095-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492-
0.0102-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487-
0.015-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487-
0.0154-(2Z,6E,10E)-geranylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474-
0.019-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487-
0.023-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C637492-
5.3-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-S74A mutant, pH 7.3, 37°C637491-
5.8-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E216Q mutant, pH 7.3, 37°C637491-
6-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R197S mutant, pH 7.3, 37°C637491-
7.5-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-D226A mutant, pH 7.3, 37°C637491-
8.1-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E193Q mutant, pH 7.3, 37°C; R203S mutant, pH 7.3, 37°C637491-
8.2-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild type, pH 7.3, 37°C637491-
9.4-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-F73A mutant, pH 7.3, 37°C637491-
17.7-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E201Q mutant, pH 7.3, 37°C637491-
18.1-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-D221A mutant, pH 7.3, 37°C637491-
0.0588-(2Z,6E,10E,14E)-farnesylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474-
0.0526-(2Z,6Z,10E,14E)-farnesylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474-
0.00017-(E,E)-(2-Diazo-3-trifluoropropionyloxy)geranyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637478 2D-image
0.00013-(E,E)-Farnesyl diphosphateLactobacillus plantarumQ88VJ8pH 7.5, 35°C637473 2D-image
0.00013-(E,E)-Farnesyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637475, 637478 2D-image
0.007-(E,E)-Farnesyl diphosphateMicrococcus luteus-pH 7.4, 35°C637481 2D-image
0.008-(E,E)-Farnesyl diphosphateMicrococcus luteus--637475 2D-image
0.0091-(E,E)-Farnesyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.0091-(E,E)-Farnesyl diphosphateBacillus subtilis--637475 2D-image
0.103-(E,E)-Farnesyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.008-(E,E,E)-geranylgeranyl diphosphateMicrococcus luteus-pH 7.5, 35°C637481 2D-image
0.0093-(E,E,E)-geranylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.037-(E,E,E)-geranylgeranyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.0189-(Z,E)-farnesyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.305-(Z,E)-farnesyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.0023-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme E76Q, pH 7.5, 37°C637492 2D-image
0.0043-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme G32R, pH 7.5, 37°C637492 2D-image
0.0045-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme R42G, pH 7.5, 37°C637492 2D-image
0.005-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.005-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme D29A, pH 7.5, 37°C637492 2D-image
0.0053-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme S74A, pH 7.3, 37°C637491 2D-image
0.0058-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme R216Q, pH 7.3, 37°C637491 2D-image
0.0059-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme G32R/R42G, pH 7.5, 37°C637492 2D-image
0.006-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme R197S, pH 7.3, 37°C637491 2D-image
0.006-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme E84Q, pH 7.5, 37°C637492 2D-image
0.0061-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme R80A, pH 7.5, 37°C637492 2D-image
0.008-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C; mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.0081-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme E193Q, pH 7.3, 37°C; mutant enzyme R203S, pH 7.3, 37°C637491 2D-image
0.0082-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487 2D-image
0.0082-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.3, 37°C637491 2D-image
0.0082-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637492 2D-image
0.0094-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme F73A, pH 7.3, 37°C637491 2D-image
0.0095-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme R33A, pH 7.5, 37°C637492 2D-image
0.0102-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.015-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
0.0154-(Z,E,E)-Geranylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.0177-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme E201Q, pH 7.3, 37°C637491 2D-image
0.0181-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme D221A, pH 7.3, 37°C637491 2D-image
0.019-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.134-(Z,E,E)-Geranylgeranyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.0588-(Z,E,E,E)-farnesylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.0526-(Z,Z,E,E)-farnesylgeranyl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.00069-7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one geranyl diphosphateEscherichia coli-alternative substrate, pH 7.5, 25°C708864-
0.00011-farnesyl diphosphateHelicobacter pyloriP55984wild-type, pH 7.5699031 2D-image
0.00015-farnesyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5699031 2D-image
0.0003-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A659232 2D-image
0.0004-farnesyl diphosphateEscherichia coli-wild-type enzyme, pH 7.5, 25°C637485 2D-image
0.0004-farnesyl diphosphateEscherichia coli-mutant enzyme E73A, N74A and E81A, pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637493 2D-image
0.0004-farnesyl diphosphateEscherichia coli-mutant enzyme W91F, pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637494 2D-image
0.0004-farnesyl diphosphateEscherichia coli-mutant enzymes E73A, D150A and D218A, pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637495 2D-image
0.0004-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme657857 2D-image
0.0004-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232 2D-image
0.0004-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme659476 2D-image
0.00046-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26K659476 2D-image
0.0005-farnesyl diphosphateEscherichia coli-mutant enzyme W221F, pH 7.5, 25°C637494 2D-image
0.0005-farnesyl diphosphateEscherichia coli-mutant enzyme D26A, pH 7.5, 25°C637495 2D-image
0.0005-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232 2D-image
0.0005-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26A659476 2D-image
0.00055-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26R659476 2D-image
0.00066-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A/E213A659232 2D-image
0.00067-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26E659476 2D-image
0.0007-farnesyl diphosphateEscherichia coli-pH 7.5, 30°C637482 2D-image
0.0007-farnesyl diphosphateEscherichia coli-mutant enzyme W149F, pH 7.5, 25°C637494 2D-image
0.0007-farnesyl diphosphateEscherichia coli-mutant enzyme E213A, pH 7.5, 25°C637495 2D-image
0.0007-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant E213A659232 2D-image
0.001-farnesyl diphosphateEscherichia coli-mutant enzyme S71A, pH 7.5, 25°C637493 2D-image
0.0015-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant W210A659084 2D-image
0.0016-farnesyl diphosphateEscherichia coli-mutant enzyme R77A, pH 7.5, 25°C637493 2D-image
0.0016-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant L85A657857 2D-image
0.0018-farnesyl diphosphateEscherichia coli-mutant enzyme W75F, pH 7.5, 25°C637494 2D-image
0.002-farnesyl diphosphateEscherichia coli-mutant enzyme W31F, pH 7.5, 25°C637494 2D-image
0.0021-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant L88A657857 2D-image
0.0023-farnesyl diphosphateMicrococcus luteus-mutant enzyme E76Q, pH 7.5, 37°C637492 2D-image
0.0026-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant F89A657857 2D-image
0.0028-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.003-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H43A659232 2D-image
0.0032-farnesyl diphosphateEscherichia coli-mutant enzyme W75A, pH 7.5, 25°C637493 2D-image
0.0033-farnesyl diphosphateMicrococcus luteus-mutant enzyme G32R, pH 7.5, 37°C637492 2D-image
0.0034-farnesyl diphosphateEscherichia coli-mutant enzyme W207F, pH 7.5, 25°C637494 2D-image
0.0035-farnesyl diphosphateMicrococcus luteus-mutant enzyme D221A, pH 7.3, 37°C637491 2D-image
0.0036-farnesyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637492 2D-image
0.0049-farnesyl diphosphateMicrococcus luteus-mutant enzyme R42G, pH 7.5, 37°C637492 2D-image
0.005-farnesyl diphosphateMicrococcus luteus-mutant enzyme G32R/R42G, pH 7.5, 37°C637492 2D-image
0.0054-farnesyl diphosphateMicrococcus luteus-mutant enzyme R216Q, pH 7.3, 37°C637491 2D-image
0.0066-farnesyl diphosphateMicrococcus luteus-mutant enzyme E193Q, pH 7.3, 37°C637491 2D-image
0.0077-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y71S659084 2D-image
0.0083-farnesyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637487 2D-image
0.0083-farnesyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.3, 37°C637491 2D-image
0.0083-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant wild-type enzyme659084 2D-image
0.0083-farnesyl diphosphateMicrococcus luteus-wild type enzyme673574 2D-image
0.0092-farnesyl diphosphateMicrococcus luteus-mutant enzyme F73A, pH 7.3, 37°C637491 2D-image
0.0093-farnesyl diphosphateMicrococcus luteus-mutant enzyme F73A673574 2D-image
0.0096-farnesyl diphosphateMicrococcus luteus-mutant enzyme S74A, pH 7.3, 37°C637491 2D-image
0.0104-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.0112-farnesyl diphosphateMicrococcus luteus-mutant enzyme D226A, pH 7.3, 37°C637491 2D-image
0.0114-farnesyl diphosphateMicrococcus luteus-mutant enzyme E84Q, pH 7.5, 37°C637492 2D-image
0.0116-farnesyl diphosphateMicrococcus luteus-mutant enzyme E201Q, pH 7.3, 37°C637491 2D-image
0.0136-farnesyl diphosphateMicrococcus luteus-mutant enzyme R203S, pH 7.3, 37°C637491 2D-image
0.0139-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.014-farnesyl diphosphateMicrococcus luteus-mutant enzyme A72L/F73L/W78L673574 2D-image
0.0147-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.018-farnesyl diphosphateMicrococcus luteus-mutant enzyme R197S, pH 7.3, 37°C637491 2D-image
0.022-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant F207S659084 2D-image
0.0231-farnesyl diphosphateMicrococcus luteus-mutant enzyme R80A, pH 7.5, 37°C637492 2D-image
0.026-farnesyl diphosphateMicrococcus luteus-mutant enzyme A72L/F73L673574 2D-image
0.0332-farnesyl diphosphateMicrococcus luteus-mutant enzyme D29A, pH 7.5, 37°C637492 2D-image
0.0495-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.1207-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
0.144-farnesyl diphosphateMicrococcus luteus-mutant enzyme R33A, pH 7.5, 37°C637492 2D-image
0.155-farnesyl diphosphateMicrococcus luteus-mutant enzyme N78D, pH 7.5, 37°C637487 2D-image
0.0032-geranyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.036-geranyl diphosphateEscherichia coli-25°C, pH 7.5657857 2D-image
0.0003-geranylgeranyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme; wild type, 25°C, pH 7.5657857 2D-image
0.0007-geranylgeranyl diphosphateEscherichia coli-L88A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant L88A657857 2D-image
0.001-geranylgeranyl diphosphateEscherichia coli-F89A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant F89A657857 2D-image
0.0012-geranylgeranyl diphosphateEscherichia coli-L85A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant L85A657857 2D-image
0.0075-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme D226A, pH 7.3, 37°C637491 2D-image
0.00041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme659476 2D-image
0.0009-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26K659476 2D-image
0.0014-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26A659476 2D-image
0.00192-isopentenyl diphosphateLactobacillus plantarumQ88VJ8pH 7.5, 35°C; pH 7.5, 35°C637473 2D-image
0.00192-isopentenyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637475, 637478 2D-image
0.0021-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26E659476 2D-image
0.0022-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26R659476 2D-image
0.004-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C637485 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C; pH 7.5, 25°C, wild type637493 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-wild-type enzyme, pH 7.5, 25°C637494 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C; pH 7.5, 25°C, wild type637495 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme, with farnesyl diphosphate; wild type, with (2E,6E)-farnesyl diphosphate, 25°C, pH 7.5657857 2D-image
0.0041-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type659232, 707467 2D-image
0.0044-isopentenyl diphosphateEscherichia coli-mutant enzyme D218A, pH 7.5, 25°C637495 2D-image
0.0059-isopentenyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C; mutant enzyme G32R/R42G, pH 7.5, 37°C637492 2D-image
0.0059-isopentenyl diphosphateEscherichia coli-mutant enzyme W31F, pH 7.5, 25°C637494 2D-image
0.006-isopentenyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C; mutant enzyme G32R, pH 7.5, 37°C637492 2D-image
0.0072-isopentenyl diphosphateEscherichia coli-mutant enzyme W91F, pH 7.5, 25°C637494 2D-image
0.0078-isopentenyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487 2D-image
0.0078-isopentenyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.3, 37°C637491 2D-image
0.0078-isopentenyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C; wild-type, pH 7.5, 37°C637492 2D-image
0.0078-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant wild-type enzyme; pH 7.5, 30°C, wild type659084 2D-image
0.0078-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)5 mutant707467 2D-image
0.008-isopentenyl diphosphateEscherichia coli-mutant enzyme N74A, pH 7.5, 25°C; pH 7.5, 25°C, N74A mutant637493 2D-image
0.0085-isopentenyl diphosphateBacillus subtilis-37°C, pH 37°C708500 2D-image
0.009-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.0092-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, D26K mutant with 0.5 mM MgCl2659476 2D-image
0.0092-isopentenyl diphosphateHelicobacter pyloriP55984wild-type, pH 7.5699031 2D-image
0.0092-isopentenyl diphosphateHelicobacter pylori-wild-type704720 2D-image
0.0096-isopentenyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5699031 2D-image
0.0096-isopentenyl diphosphateHelicobacter pylori-mutant C234A704720 2D-image
0.0097-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 1 mM MgCl2659476 2D-image
0.0114-isopentenyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C; mutant enzyme E76Q, pH 7.5, 37°C637492 2D-image
0.0115-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 0.05 mM MgCl2659476 2D-image
0.0117-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAS72 mutant707467 2D-image
0.012-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.013-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme, with geranylgeranyl diphosphate; wild type, with geranylgeranyl diphosphate, 25°C, pH 7.5657857 2D-image
0.0131-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.014-isopentenyl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
0.014-isopentenyl diphosphateEscherichia coli-mutant enzyme W221F, pH 7.5, 25°C637494 2D-image
0.014-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232 2D-image
0.0141-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.0141-isopentenyl diphosphateEscherichia coli-mutant enzyme D26A, pH 7.5, 25°C637495 2D-image
0.0141-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, D26A mutant659232 2D-image
0.015-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.0157-isopentenyl diphosphateEscherichia coli-mutant enzyme R77A, pH 7.5, 25°C; pH 7.5, 25°C, R77A mutant637493 2D-image
0.0157-isopentenyl diphosphateEscherichia coli-mutant enzyme R77A, pH 7.5, 25°C637495 2D-image
0.016-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, H199A mutant; pH 7.5, 25°C, recombinant mutant H199A659232 2D-image
0.0162-isopentenyl diphosphateEscherichia coli-mutant enzyme E73A, pH 7.5, 25°C; pH 7.5, 25°C, E73A mutant637493 2D-image
0.0162-isopentenyl diphosphateEscherichia coli-; pH 7.5, 25°C, wild type637495 2D-image
0.0165-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
0.017-isopentenyl diphosphateMicrococcus luteus-mutant enzyme D4226A, pH 7.3, 37°C637491 2D-image
0.0175-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, W210A mutant659084 2D-image
0.0175-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 3 mM MgCl2659476 2D-image
0.0177-isopentenyl diphosphateMicrococcus luteus-mutant enzyme D221A, pH 7.3, 37°C637491 2D-image
0.018-isopentenyl diphosphateEscherichia coli-F89A mutant, with geranylgeranyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant F89A, with geranylgeranyl diphosphate657857 2D-image
0.018-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant W210A659084 2D-image
0.0183-isopentenyl diphosphateMicrococcus luteus-mutant enzyme E201Q, pH 7.3, 37°C637491 2D-image
0.02-isopentenyl diphosphateEscherichia coli-mutant enzyme W149F, pH 7.5, 25°C637494 2D-image
0.0204-isopentenyl diphosphateMicrococcus luteus-mutant enzyme E193Q, pH 7.3, 37°C637491 2D-image
0.0208-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, D26E mutant with 0.5 mM MgCl2659476 2D-image
0.0223-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, D26R mutant with 0.5 mM MgCl2659476 2D-image
0.0229-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, Y148F mutant659084 2D-image
0.023-isopentenyl diphosphateEscherichia coli-mutant enzyme W207F, pH 7.5, 25°C637494 2D-image
0.023-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.0242-isopentenyl diphosphateMicrococcus luteus-mutant enzyme R42G, pH 7.5, 37°C; R42G mutant, pH 7.5, 37°C637492 2D-image
0.0254-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, Y71S mutant659084 2D-image
0.026-isopentenyl diphosphateEscherichia coli-mutant enzyme W75F, pH 7.5, 25°C637494 2D-image
0.026-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y71S659084 2D-image
0.027-isopentenyl diphosphateSaccharomyces cerevisiae--637486 2D-image
0.029-isopentenyl diphosphateEscherichia coli-pH 7.5, 30°C637482 2D-image
0.0307-isopentenyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C; mutant enzyme E84Q, pH 7.5, 37°C637492 2D-image
0.034-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)1 mutant707467 2D-image
0.0356-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, W224A mutant659084 2D-image
0.036-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.042-isopentenyl diphosphateEscherichia coli-L88A mutant, with geranylgeranyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant L88A, with geranylgeranyl diphosphate657857 2D-image
0.0452-isopentenyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C; mutant enzyme D29A, pH 7.5, 37°C637492 2D-image
0.046-isopentenyl diphosphateEscherichia coli-mutant enzyme W75A, pH 7.5, 25°C; pH 7.5, 25°C, W75A mutant637493 2D-image
0.0491-isopentenyl diphosphateMicrococcus luteus-mutant enzyme R80A, pH 7.5, 37°C; R80A mutant, pH 7.5, 37°C637492 2D-image
0.0561-isopentenyl diphosphateMicrococcus luteus-mutant enzyme R197S, pH 7.3, 37°C637491 2D-image
0.06-isopentenyl diphosphateEscherichia coli-L85A mutant, with geranylgeranyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant L85A, with geranylgeranyl diphosphate657857 2D-image
0.0621-isopentenyl diphosphateMicrococcus luteus-mutant enzyme R203S, pH 7.3, 37°C637491 2D-image
0.063-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, H43A mutant; pH 7.5, 25°C, recombinant mutant H43A659232 2D-image
0.084-isopentenyl diphosphateEscherichia coli-F89A mutant, with (2E,6E)-farnesyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant F89A, with farnesyl diphosphate657857 2D-image
0.088-isopentenyl diphosphateEscherichia coli-mutant enzyme E81A, pH 7.5, 25°C; pH 7.5, 25°C, E81A mutant637493 2D-image
0.0909-isopentenyl diphosphateMicrococcus luteus-mutant enzyme E216Q, pH 7.3, 37°C637491 2D-image
0.103-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant F207S659084 2D-image
0.1031-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, F207S mutant659084 2D-image
0.1268-isopentenyl diphosphateMicrococcus luteus-mutant enzyme S74A, pH 7.3, 37°C637491 2D-image
0.133-isopentenyl diphosphateEscherichia coli-mutant enzyme S71A, pH 7.5, 25°C; pH 7.5, 25°C, S71A mutant637493 2D-image
0.173-isopentenyl diphosphateEscherichia coli-L88A mutant, with (2E,6E)-farnesyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant L88A, with farnesyl diphosphate657857 2D-image
0.2525-isopentenyl diphosphateMicrococcus luteus-mutant enzyme F73A, pH 7.3, 37°C637491 2D-image
0.27-isopentenyl diphosphateEscherichia coli-mutant enzyme D150A, pH 7.5, 25°C637495 2D-image
0.279-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, H199A/E213A mutant; pH 7.5, 25°C, recombinant mutant H199A/E213A659232 2D-image
0.28-isopentenyl diphosphateEscherichia coli-mutant enzyme D213A, pH 7.5, 25°C637495 2D-image
0.28-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, E213A mutant; pH 7.5, 25°C, recombinant mutant E213A659232 2D-image
0.291-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 50 mM MgCl2659476 2D-image
0.617-isopentenyl diphosphateEscherichia coli-L85A mutant, with (2E,6E)-farnesyl diphosphate, 25°C, pH 7.5; pH 7.5, 25°C, mutant L85A, with farnesyl diphosphate657857 2D-image
7.8-isopentenyl diphosphateMicrococcus luteus-wild type, pH 7.3, 37°C637491 2D-image
17-isopentenyl diphosphateMicrococcus luteus-D226A mutant, pH 7.3, 37°C637491 2D-image
17.7-isopentenyl diphosphateMicrococcus luteus-D221A mutant, pH 7.3, 37°C637491 2D-image
18.3-isopentenyl diphosphateMicrococcus luteus-E201Q mutant, pH 7.3, 37°C637491 2D-image
20.4-isopentenyl diphosphateMicrococcus luteus-E193Q mutant, pH 7.3, 37°C637491 2D-image
56.1-isopentenyl diphosphateMicrococcus luteus-R197S mutant, pH 7.3, 37°C637491 2D-image
62.1-isopentenyl diphosphateMicrococcus luteus-R203S mutant, pH 7.3, 37°C637491 2D-image
90.9-isopentenyl diphosphateMicrococcus luteus-E216Q mutant, pH 7.3, 37°C637491 2D-image
126.8-isopentenyl diphosphateMicrococcus luteus-S74A mutant, pH 7.3, 37°C637491 2D-image
0.0267-neryl diphosphateBacillus subtilis-pH 8.5, 37°C637474 2D-image
0.032-neryl diphosphateLactobacillus plantarum-pH 7.5, 35°C637483 2D-image
252.5-isopentenyl diphosphateMicrococcus luteus-F73A mutant, pH 7.3, 37°C637491 2D-image
additional information-additional informationEscherichia coli-steady-state kinetics, single turnover measurements with substrate geranylgeranyl diphosphate657857-
additional information-additional informationEscherichia coli-steady-state kinetics659232-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
6.33e-05-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26R mutant with 0.5 mM MgCl2659476 2D-image
7.66e-05-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26K mutant with 0.5 mM MgCl2659476 2D-image
0.00013-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)5 mutant707467 2D-image
0.00014-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, R77A mutant637493 2D-image
0.00022-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAV82S83 mutant707467 2D-image
0.00028-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAS72 mutant707467 2D-image
0.000366-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26E mutant with 0.5 mM MgCl2659476 2D-image
0.00076-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, DELTAS83 mutant707467 2D-image
0.0009-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S83(Ala)1 mutant707467 2D-image
0.00125-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.00155-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.0025-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A/E213A659232 2D-image
0.0026-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H43A and mutant E213A659232 2D-image
0.00272-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.0033-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme D26A, pH 7.5, 25°C637495 2D-image
0.0033-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232 2D-image
0.004-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C637492 2D-image
0.013-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, without 0.1% Triton637485 2D-image
0.0167-(2E,6E)-farnesyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C637492 2D-image
0.022-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, N74A mutant637493 2D-image
0.026-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme E213A, pH 7.5, 25°C637495 2D-image
0.0542-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492 2D-image
0.095-(2E,6E)-farnesyl diphosphateEscherichia coli-L85A mutant, 25°C, pH 7.5657857 2D-image
0.11-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S71A mutant637493 2D-image
0.151-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.2-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5, temperature not specified in the publication699031 2D-image
0.2-(2E,6E)-farnesyl diphosphateHelicobacter pylori-mutant C234A, co-substrate: isopentenyl diphosphate704720 2D-image
0.216-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C637492 2D-image
0.22-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme D218A, pH 7.5, 25°C637495 2D-image
0.22-(2E,6E)-farnesyl diphosphateHelicobacter pyloriP55984wild type, pH 7.5, temperature not specified in the publication699031 2D-image
0.22-(2E,6E)-farnesyl diphosphateHelicobacter pylori-wild-type, co-substrate: isopentenyl diphosphate704720 2D-image
0.23-(2E,6E)-farnesyl diphosphateEscherichia coli-L88A mutant, 25°C, pH 7.5657857 2D-image
0.3-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E73A mutant637493 2D-image
0.3-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzymes E73A, pH 7.5, 25°C637495 2D-image
0.4-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E81A mutant637493 2D-image
0.434-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme N78R, pH 7.5, 37°C637487 2D-image
0.456-(2E,6E)-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.462-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C637492 2D-image
0.505-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C637492 2D-image
0.61-(2E,6E)-farnesyl diphosphateEscherichia coli-F89A mutant, 25°C, pH 7.5657857 2D-image
0.96-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C637492 2D-image
1.09-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C637492 2D-image
1.1-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, W75A mutant637493 2D-image
1.1-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W31F, pH 7.5, 25°C; mutant enzyme W75F, pH 7.5, 25°C637494 2D-image
1.1-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme D150A, pH 7.5, 25°C637495 2D-image
1.22-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487 2D-image
1.23-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 0.05 mM MgCl2659476 2D-image
1.5-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W207F, pH 7.5, 25°C637494 2D-image
1.66-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492 2D-image
1.7-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W149F, pH 7.5, 25°C637494 2D-image
1.92-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 3 mM MgCl2659476 2D-image
1.98-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 1 mM MgCl2659476 2D-image
2.2-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A659232 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, in the presence of 0.1% Triton637485 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type637493 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W91F, pH 7.5, 25°C; wild-type enzyme, pH 7.5, 25°C637494 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-wild type, pH 7.5, 25°C637495 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-wild type, 25°C, pH 7.5657857 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232 2D-image
2.5-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type707467 2D-image
3.5-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W221F, pH 7.5, 25°C637494 2D-image
3.1e-07-(2E,6E)-farnesyl thiodiphosphateEscherichia coli-much smaller than using (2E,6E)-farnesyl diphosphate, pH 7.5, 25°C637494-
0.002-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487-
0.00231-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487-
0.00415-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487-
0.00579-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C637492-
0.0258-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C637492-
0.0813-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492-
0.3-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487-
0.382-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C637492-
0.604-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C637492-
0.608-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C637492-
0.899-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487-
1.07-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C637492-
1.11-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C637492-
1.37-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487-
1.77-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487-
1.77-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492-
0.002-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.00231-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.00415-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.3-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.899-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
1.37-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
1.77-(Z,E,E)-Geranylgeranyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487 2D-image
0.02-7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one geranyl diphosphateEscherichia coli-alternative substrate, pH 7.5, 25°C708864-
6e-05-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26R659476 2D-image
8e-05-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26K659476 2D-image
0.0004-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26E659476 2D-image
0.00125-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.00155-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.002-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant W210A659084 2D-image
0.0025-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A/E213A659232 2D-image
0.0026-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H43A and mutant E213A659232 2D-image
0.00272-farnesyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.003-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant F207S659084 2D-image
0.0033-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232 2D-image
0.0033-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant D26A659476 2D-image
0.015-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.0167-farnesyl diphosphateMicrococcus luteus-mutant enzyme D29A, pH 7.5, 37°C637492 2D-image
0.0542-farnesyl diphosphateMicrococcus luteus-mutant enzyme R33A, pH 7.5, 37°C637492 2D-image
0.071-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.095-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant L85A657857 2D-image
0.11-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y71S659084 2D-image
0.151-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.2-farnesyl diphosphateHelicobacter pyloriP55984mutant C234A, pH 7.5699031 2D-image
0.216-farnesyl diphosphateMicrococcus luteus-mutant enzyme R42G, pH 7.5, 37°C637492 2D-image
0.22-farnesyl diphosphateHelicobacter pyloriP55984wild-type, pH 7.5699031 2D-image
0.23-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant L88A657857 2D-image
0.434-farnesyl diphosphateMicrococcus luteus-mutant enzyme N78R, pH 7.5, 37°C637487 2D-image
0.456-farnesyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.462-farnesyl diphosphateMicrococcus luteus-mutant enzyme G32R, pH 7.5, 37°C637492 2D-image
0.505-farnesyl diphosphateMicrococcus luteus-mutant enzyme E76Q, pH 7.5, 37°C637492 2D-image
0.61-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, mutant F89A657857 2D-image
0.96-farnesyl diphosphateMicrococcus luteus-mutant enzyme G32R/R42G, pH 7.5, 37°C637492 2D-image
1.09-farnesyl diphosphateMicrococcus luteus-mutant enzyme E84Q, pH 7.5, 37°C637492 2D-image
1.22-farnesyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637487 2D-image
1.22-farnesyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant wild-type enzyme659084 2D-image
1.66-farnesyl diphosphateMicrococcus luteus-wild-type enzyme, pH 7.5, 37°C637492 2D-image
2.2-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A659232 2D-image
2.5-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme657857 2D-image
2.5-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232 2D-image
2.5-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme659476 2D-image
1.7-geranyl diphosphateEscherichia coli-25°C, pH 7.5657857 2D-image
0.18-geranylgeranyl diphosphateEscherichia coli-L85A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant L85A657857 2D-image
0.32-geranylgeranyl diphosphateEscherichia coli-L88A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant L88A657857 2D-image
0.7-geranylgeranyl diphosphateEscherichia coli-F89A mutant, 25°C, pH 7.5; pH 7.5, 25°C, mutant F89A657857 2D-image
2.1-geranylgeranyl diphosphateEscherichia coli-pH 7.5, 25°C, wild-type enzyme; wild type, 25°C, pH 7.5657857 2D-image
0.0002-isopentenyl diphosphateSaccharomyces cerevisiae--637486 2D-image
0.002-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant W210A659084 2D-image
0.0025-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A/E213A659232 2D-image
0.0026-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H43A and mutant E213A659232 2D-image
0.0027-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77Q, pH 7.5, 37°C637487 2D-image
0.0033-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232 2D-image
0.00473-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77D, pH 7.5, 37°C637487 2D-image
0.01-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant F207S659084 2D-image
0.0164-isopentenyl diphosphateMicrococcus luteus-mutant enzyme N77A, pH 7.5, 37°C637487 2D-image
0.071-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.11-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y71S659084 2D-image
0.115-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant mutant Y148F659084 2D-image
0.2-isopentenyl diphosphateHelicobacter pylori-mutant C234A, co-substrate: farnesyl diphosphate704720 2D-image
0.22-isopentenyl diphosphateHelicobacter pylori-wild-type, co-substrate: farnesyl diphosphate704720 2D-image
0.397-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78D, pH 7.5, 37°C637487 2D-image
0.783-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78I, pH 7.5, 37°C637487 2D-image
0.803-isopentenyl diphosphateMicrococcus luteus-mutant enzyme W78R, pH 7.5, 37°C637487 2D-image
1.55-isopentenyl diphosphateMicrococcus luteus-pH 7.5, 30°C, recombinant wild-type enzyme659084 2D-image
1.85-isopentenyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637487 2D-image
2.2-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A659232 2D-image
2.5-isopentenyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232 2D-image
additional information-additional informationSaccharomyces cerevisiae--637486-
additional information-additional informationMicrococcus luteus--637491-
additional information-additional informationEscherichia coli--637493, 637494, 637495-
additional information-additional informationMicrococcus luteus-turnover number for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A659084-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0875-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, R77A mutant637493263972
0.1151-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26R mutant with 0.5 mM MgCl2659476263972
0.1665-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26K mutant with 0.5 mM MgCl2659476263972
0.25-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C637492263972
0.5462-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, D26E mutant with 0.5 mM MgCl2659476263972
0.713-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C637492263972
0.777-(2E,6E)-farnesyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C637492263972
0.866-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H43A659232263972
3.79-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A/E213A659232263972
6.25-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant wild-type enzyme659232263972
6.6-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant D26A659232263972
7.86-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant H199A659232263972
37.14-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, recombinant mutant E213A659232263972
55-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, N74A mutant637493263972
77.9-(2E,6E)-farnesyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C637492263972
93.9-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C637492263972
110-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, S71A mutant637493263972
184-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C637492263972
222-(2E,6E)-farnesyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C637492263972
262-(2E,6E)-farnesyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C637492263972
344-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, W75A mutant637493263972
347-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W91F, pH 7.5, 25°C637494263972
441-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W207F, pH 7.5, 25°C637494263972
461-(2E,6E)-farnesyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C637492263972
550-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W31F, pH 7.5, 25°C637494263972
611-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W75F, pH 7.5, 25°C637494263972
750-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E73A mutant637493263972
820-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 0.05 mM MgCl2659476263972
1000-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, E81A mutant637493263972
2428-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W149F, pH 7.5, 25°C637494263972
4363-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 3 mM MgCl2659476263972
5351-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type with 1 mM MgCl2659476263972
6250-(2E,6E)-farnesyl diphosphateEscherichia coli-pH 7.5, 25°C, wild type637493263972
6250-(2E,6E)-farnesyl diphosphateEscherichia coli-wild-type enzyme, pH 7.5, 25°C637494263972
7000-(2E,6E)-farnesyl diphosphateEscherichia coli-mutant enzyme W221F, pH 7.5, 25°C637494263972
0.949-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R80A mutant, pH 7.5, 37°C6374920
5.2-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-D29A mutant, pH 7.5, 37°C6374920
8.65-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R33A mutant, pH 7.5, 37°C6374920
26.3-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E76Q mutant, pH 7.5, 37°C6374920
84.8-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-R42G mutant, pH 7.5, 37°C6374920
141-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R mutant, pH 7.5, 37°C6374920
178-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-E84Q mutant, pH 7.5, 37°C6374920
188-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-G32R/R42G mutant, pH 7.5, 37°C6374920
215.9-(2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-wild-type, pH 7.5, 37°C6374920
additional information-additional informationMicrococcus luteus-kcat/KM-values for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A6590840

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0002-(2E,6E)-farnesyl thiodiphosphateEscherichia coli-pH 7.5, 25°C637494-
0.008-(2E,6E,10E)-4-methylfarnesyl diphosphateBacillus subtilis-competitive inhibitor against (2Z,6E,10E)-geranylgeranyl diphosphate, 37°C, pH 37°C708500-
0.0054-(2Z,6E,10E)-4-methyl-geranylgeranyl diphosphateBacillus subtilis-potent competitive inhibitor against (2Z,6E,10E)-geranylgeranyl diphosphate, 37°C, pH 37°C708500-
0.0058-(2Z,6E,10E)-4-methyl-geranylgeranyl diphosphateBacillus subtilis-noncompetitive inhibitor against isopentenyl diphosphate, 37°C, pH 37°C708500-
0.041-(E)-3-methyl-3-pentenyl diphosphateBacillus subtilis-calculated against isopentenyl diphosphate, 37°C, pH 37°C708500-
0.075-(E)-3-methyl-3-pentenyl diphosphateBacillus subtilis-calculated against (2Z,6E,10E)-geranylgeranyl diphosphate, 37°C, pH 37°C708500-
0.0002-(S)-farnesyl thiopyrophosphateEscherichia coli--637494 2D-image
0.017-3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-substrate farnesyl diphosphate, pH 7.5, 37°C685691-
0.028-3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphateMicrococcus luteus-substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C685691-
0.045-3-desmethyl farnesyl diphosphateMicrococcus luteus-substrate farnesyl diphosphate, pH 7.5, 37°C685691 2D-image
2.8-3-desmethyl farnesyl diphosphateMicrococcus luteus-substrate (2Z,6E,10E)-geranylgeranyl diphosphate, pH 7.5, 37°C; substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C685691 2D-image
0.017-3-desmethyl Z-geranylgeranyl diphosphateMicrococcus luteus-substrate farnesyl diphosphate, pH 7.5, 37°C685691 2D-image
0.028-3-desmethyl Z-geranylgeranyl diphosphateMicrococcus luteus-substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C685691 2D-image
0.00057-7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one geranyl diphosphateEscherichia coli-(2E,6E)-farnesyl diphosphate as a substrate, pH 7.5, 25°C708864-
1.1-Mg2+Escherichia coli-pH 7.5, 25°C; pH 7.5, 25°C659476 2D-image
17-SO42-Micrococcus luteus--637492 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.071-3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideEscherichia coli--704720 2D-image
0.362-3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideHelicobacter pyloriP55984pH 7.5; pH 7.5, temperature not specified in the publication699031 2D-image
0.362-3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamideHelicobacter pylori-IC50 value of this compound is equal against the C234A mutant and wild-type704720 2D-image
0.00063-5-benzyl-4-hydroxy-5-methyl-2-oxo-2,5-dihydro-1H-pyrrole-3-carboxylic acid (4-cyclohexylphenyl)amideStreptococcus pneumoniae-pH 7.3, temperature not specified in the publication, N-(4-benzoylphenyl)-4-hydroxy-2-oxo-5-phenethyl-2,5-dihydro-1H-pyrrole-3-carboxamide as substrate707529-
0.071-N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideEscherichia coli-pH 7.5; pH 7.5, temperature not specified in the publication699031 2D-image
0.071-N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideEscherichia coli--704720 2D-image
0.35-N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideHelicobacter pyloriP55984pH 7.5; pH 7.5, temperature not specified in the publication699031 2D-image
0.35-N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamideHelicobacter pylori-IC50 value of this compound is equal against the C234A mutant and wild-type704720 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.000424-Bacillus subtilis-; pH 8.5, 37°C637474
0.004066-Micrococcus luteus--637481
0.013-Escherichia coli-pH 7.5, 25°C, absence of Triton637485
1.534-Micrococcus luteus-; pH 7.5, 37°C637488
2.5-Escherichia coli-pH 7.5, 25°C, in presence of 0.1% Triton637485
additional information-Lactobacillus plantarumQ88VJ8-637473
additional information-Lactobacillus plantarum--637475, 637480
additional information-Micrococcus luteus--659084

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.3-Micrococcus luteus-assay at637491
7.4-Micrococcus luteus-assay at637476
7.59Escherichia coli--637482
7.5-Lactobacillus plantarum-and a second optimum at pH 10.2, that is 40% of the optimum at pH 7.5637475
7.5-Micrococcus luteus--637475
7.5-Lactobacillus plantarum-and a second optimum at pH 10.2, that is 40% of the optimum at pH 7.5637480
7.5-Micrococcus luteus--637481
7.5-Escherichia coli-assay at637485
7.5-Micrococcus luteus-assay at637492
7.5-Escherichia coli-assay at637494, 657857
7.5-Micrococcus luteus-assay at; assay at659084
7.5-Escherichia coli-assay at659232
7.5-Escherichia coli-assay at; assay at659476
7.5-Micrococcus luteus-assay at685691
7.5-Escherichia coli-assay at699031
7.5-Helicobacter pyloriP55984assay at699031
7.5-Escherichia coli-assay at704720, 708864, 708911
8.5-Bacillus subtilis-; assay at637474
8.5-Bacillus subtilis--637475
8.5-Bacillus subtilis-assay at708500
10.2-Lactobacillus plantarum-and a second optimum at pH 7.5 that is higher than the optimum at pH 10.2637475, 637480

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
7.59Micrococcus luteus-pH 7.5: activity maximum, pH 9.0: about 80% of maximal activity637481

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Escherichia coli-assay at637485, 637494, 657857, 659232
25-Escherichia coli-assay at; assay at659476
25-Escherichia coli-assay at708864
30-Escherichia coli-assay at637482
30-Micrococcus luteus-assay at; assay at659084
3545Lactobacillus plantarum--637480
37-Bacillus subtilis-assay at637474
37-Micrococcus luteus-assay at637476, 637491, 637492, 685691
37-Bacillus subtilis-assay at708500

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.1-Lactobacillus plantarumQ88VJ8-637473

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolEscherichia coli--5829637479Manually annotated by BRENDA team
solubleLactobacillus plantarum---637477, 637484Manually annotated by BRENDA team
solubleMicrococcus luteus---637481Manually annotated by BRENDA team
membraneMicrococcus luteus--16020637488Manually annotated by BRENDA team
additional informationSaccharomyces cerevisiae-the recombinant enzyme expressed in Escherichia coli mostly exists in pellet in the absence of detergents, a low quantity of soluble enzyme is purified-637486Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3ugs, downloadSCOP (3ugs)CATH (3ugs)Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
1jp3, downloadSCOP (1jp3)CATH (1jp3)Escherichia coli (strain K12)
1ueh, downloadSCOP (1ueh)CATH (1ueh)Escherichia coli (strain K12)
1v7u, downloadSCOP (1v7u)CATH (1v7u)Escherichia coli (strain K12)
1x06, downloadSCOP (1x06)CATH (1x06)Escherichia coli (strain K12)
1x07, downloadSCOP (1x07)CATH (1x07)Escherichia coli (strain K12)
1x08, downloadSCOP (1x08)CATH (1x08)Escherichia coli (strain K12)
1x09, downloadSCOP (1x09)CATH (1x09)Escherichia coli (strain K12)
2e98, downloadSCOP (2e98)CATH (2e98)Escherichia coli (strain K12)
2e99, downloadSCOP (2e99)CATH (2e99)Escherichia coli (strain K12)
2e9a, downloadSCOP (2e9a)CATH (2e9a)Escherichia coli (strain K12)
2e9c, downloadSCOP (2e9c)CATH (2e9c)Escherichia coli (strain K12)
2e9d, downloadSCOP (2e9d)CATH (2e9d)Escherichia coli (strain K12)
3qas, downloadSCOP (3qas)CATH (3qas)Escherichia coli (strain K12)
3th8, downloadSCOP (3th8)CATH (3th8)Escherichia coli (strain K12)
2d2r, downloadSCOP (2d2r)CATH (2d2r)Helicobacter pylori (strain ATCC 700392 / 26695)
2dtn, downloadSCOP (2dtn)CATH (2dtn)Helicobacter pylori (strain ATCC 700392 / 26695)
1f75, downloadSCOP (1f75)CATH (1f75)Micrococcus luteus
2vg2, downloadSCOP (2vg2)CATH (2vg2)Mycobacterium tuberculosis
2vg3, downloadSCOP (2vg3)CATH (2vg3)Mycobacterium tuberculosis
2vg4, downloadSCOP (2vg4)CATH (2vg4)Mycobacterium tuberculosis
2h69, downloadSCOP (2h69)CATH (2h69)Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
28900-Micrococcus luteus-predicted637488
29000-Haemophilus influenzaeP44938His-tag fusion protein708911
30000-Streptococcus pneumoniae R6-His-tag fusion protein708911
31000-Escherichia coli-His-tag fusion protein708911
4700049000Micrococcus luteus-gel filtration637481
5200058000Lactobacillus plantarum-sucrose density gradient centrifugation637475
5300060000Lactobacillus plantarum-gel filtration637475, 637480
56000-Lactobacillus plantarumQ88VJ8gel filtration, sucrose density gradient centrifugation; gel filtration, sucrose density gradient centrifugation637473
56000-Lactobacillus plantarum-gel filtration, sucrose density gradient centrifugation637475
57000-Bacillus subtilis-gel filtration637474
85000-Bacillus subtilis-gel filtration637474

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerLactobacillus plantarumQ88VJ82 * 30000, SDS-PAGE; 2 * 30000, SDS-PAGE637473
dimerLactobacillus plantarum-2 * 30000, SDS-PAGE637475
dimerEscherichia coli-2 * 30000, SDS-PAGE637479
dimerEscherichia coli-alphabeta659232
dimerHelicobacter pyloriP55984each subunit contains a catalytic domain and a pairing domain699031
dimerHelicobacter pylori-crystal structure704720
dimerEscherichia coli-the two subunits show similar structures707467
homodimerMicrococcus luteus-2 * 29000, under physiological conditions637489
homodimerMicrococcus luteus-2 * 49000673055

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-676880
co-crystal structure of UPPS in complex with (2E,6E)-farnesyl diphosphateEscherichia coli-657857
hanging drop set-up; purified His-tagged wild-type enzyme, hanging drop vapour diffusion method, high concentration of sulfate or phosphate in the mother liquid to prevent binding of Triton X-100 or substrates during crystallization, 0.002 ml mother liquid containing 25% ethylene glycol, pH 7.5, mixed with 0.002 ml protein solution containing 10 mg/ml protein, 1 mM peptide, 0.05% Triton X-100, and 0.5 mM MgCl2, equilibration against 0.2 ml mother liquid at 25°C, 5 days, crystals are then soaked in mother liquid containing 0.23 mM farnesyl diphosphate, X-ray diffraction structure determination and analysis at 2.4 A resolution, modelingEscherichia coli-660464
hanging-drop method; hanging-drop methodEscherichia coli-637493
in complex with farnesyl diphosphate. Virtual screening of inhibitors from a library of 58,635 compounds, modelling of inhibitors N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamide and 3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamide into structureEscherichia coli-699031
purified His-tagged wild-type enzyme in complex with Mg2+, sulfates, and 2 molecules of Triton X-100, hanging drop vapour diffusion method, 0.002 ml protein solution containing 10 mg/ml protein, 2% Triton X-100, 5 mM MgCl2, and 0.66 mM farnesyl diphosphate, is mixed with equal volume of mother liquid containing 0.01 M CoCl2, 0.1 M MES, pH 6.5, and 1.8 M ammonium sulfate, equilibration against 0.2 ml mother liquid at 25°C, 10 days, X-ray diffraction structure determination and analysis at 1.73 A resolution, modelingEscherichia coli-659232
purified recombinant wild-type and mutant D26A enzymes in complex with Mg2+, isopentenyl diphosphate and substrate analogue farnesyl thiodiphosphate, protein solution containing 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 0.03% Triton X-100, is mixed with dried MgCl2 and isopentenyl diphosphate powder, hanging drop vapour diffusion method, 0.002 ml of the final protein solution with equal volume of mother liquor containing 20% ethylene glycol, 2-5% PEG 35000, equilibration against 0.5 ml mother liquor at room temperature, 2 days, soaking in cryoprotectant containing 2.5 mM MgCl2, 2.5 mM isopentenyl diphosphate, 30% ethylene glycol, and 5% PEG 35000 for 1 day, X-ray diffraction strcture determination and analysis at 1.9-2.2 A resolution, molecular modeling; purified recombinant wild-type and mutant D26A enzymes in complex with Mg2+, isopentenyl diphosphate and substrate analogue farnesyl thiodiphosphate, protein solution containing 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, and 0.03% Triton X-100, is mixed with dried MgCl2 and isopentenyl diphosphate powder, hanging drop vapour diffusion method, 0.002 ml of the final protein solution with equal volume of mother liquor containing 20% ethylene glycol, 2-5% PEG 35000, equilibration against 0.5 ml mother liquor at room temperature, 2 days, soaking in cryoprotectant containing 2.5 mM MgCl2, 2.5 mM isopentenyl diphosphate, 30% ethylene glycol, and 5% PEG 35000 for 1 day, X-ray diffraction strcture determination and analysis at 1.9-2.2 A resolution, molecular modelingEscherichia coli-659476
using the hanging drop setupEscherichia coli-707467
C234A UPPS mutant to prevent intra-molecular disulfide bond formed during the long period of crystallization process is crystallized using the hanging drop method. The protein is a dimer and each subunit contains a catalytic domain and a pairing domain. Two subunits are tightly associated through the central beta-sheet and a pair of long alpha-helices. Helicobacter pylori UPPS has a 1.5-turn shorter alpha5 helix in the dimer interface. This may weaken the dimer formation for Helicobacter pylori UPPS. The catalytic domain is composed of six beta-strands and four beta-helices and the central tunnel-shaped active site is surrounded by 2 alpha-helices and 4 beta-strandsHelicobacter pylori-704720
crystal structure of Helicobacter pylori UPPS and mutant by hanging drop method; in complex with farnesyl diphosphate. Virtual screening of inhibitors from a library of 58,635 compounds, modelling of inhibitors N,N'-bis(6-chloro-1,3-benzothiazol-2-yl)methanedisulfonamide and 3-[5-(5,6-dihydrobenzimidazo[1,2-c]quinazolin-6-yl)-2,5-dihydrofuran-2-yl]benzenesulfonamide into structureHelicobacter pyloriP55984699031
sitting-drop vapour-diffusion method with ammonium sulfate and lithium sulfate as precipitantsMicrococcus luteus-706947
the overall structure is determined at 2.2 A resolution by multiple isomorphous replacement with anomalous scattering; the overall structure is determined at 2.2 A resolution by multiple isomorphous replacement with anomalous scatteringMicrococcus luteus-637489

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
inactivation by irradiation with UV light in presence of (E,E)-(2-diazo-3-trifluoropropionyloxy)geranyl diphosphate, (E,E)-farnesyl diphosphate protects, isopentenyl diphosphate and Mg2+ are required for inactivation in presence of the photolabile substrateEscherichia coli-637479
inactivation by irradiation with UV light in presence of (E,E)-(2-diazo-3-trifluoropropionyloxy)geranyl diphosphate, (E,E)-farnesyl diphosphate protects, isopentenyl diphosphate and Mg2+ are required for inactivation in presence of the photolabile substrateLactobacillus plantarum-637478

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
0°C, 24 h, 56% loss of activity, partially purified enzymeBacillus subtilis-637474
-20°C, activity in enzyme preparation is stable for several weeksEscherichia coli-637482

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
partial; partially purifiedBacillus subtilis-637474
-Escherichia coli-637479, 637488, 637493, 637495, 699031, 707467
; His-tagged UPPsEscherichia coli-637485
gel chromatographyEscherichia coli-708911
partialEscherichia coli-637482
recombinant HIs-tagged wild-type and mutant enzymesEscherichia coli-659232
gel chromatographyHaemophilus influenzaeP44938708911
-Helicobacter pyloriP55984699031
-Lactobacillus plantarum-637475
; Lactobacillus plantarumQ88VJ8637473
partialLactobacillus plantarum-637477, 637480
-Micrococcus luteus-637476, 637481, 637487, 637488, 637489, 685691, 706947
-Saccharomyces cerevisiae-637486
-Streptococcus pneumoniae-707529
gel chromatographyStreptococcus pneumoniae R6-708911

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-637485, 637495, 707467, 708911
expressed in Escherichia coliEscherichia coli-704720
expressed in Escherichia coli; expression in Escherichia coliEscherichia coli-699031
expression in Escherichia coliEscherichia coli-637488
expression of mutant enzmyes W31F, W75F, W91F, W149F, W207F, and W221F as His-tag fusion proteins using Escherichia coli BL21 as host cellsEscherichia coli-637494
overexpression of His-tagged wild-type and mutant enzymesEscherichia coli-659232
overexpression of His-tagged wild-type and mutant enzymes in strain BL21(DE3)Escherichia coli-657857
-Haemophilus influenzaeP44938708911
expressed in Escherichia coliHelicobacter pylori-704720
expressed in Escherichia coli; expression in Escherichia coliHelicobacter pyloriP55984699031
-Micrococcus luteus-637489, 706947
expressed in Escherichia coliMicrococcus luteus-637487, 673574, 685691
expression in Escherichia coli, no sequence similarity between E-prenyl diphosphate and Z-prenyl diphosphate synthasesMicrococcus luteus-637488
expression of mutant enzymes R197S, R203S and E216Q in Escherichia coliMicrococcus luteus-637491
mutated enzymes are overproduced in Escherichia coli; mutated enzymes are overproduced in Escherichia coliMicrococcus luteus-637492
overexpression of wild-type and mutant enzymes in Escherichia coli strain JM109; overexpression of wild-type and mutant enzymes in Escherichia coli strain JM109Micrococcus luteus-659084
expression in Escherichia coli. Thioredoxin and His tag are utilized to increase the solubility of the recombinant protein and facilitate its purification using Ni-nitrilotriacetic acid columnSaccharomyces cerevisiae-637486
expressed in Escherichia coliStreptococcus pneumoniae-707529
-Streptococcus pneumoniae R6-708911

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
A143VEscherichia coli-the C30 intermediate is formed to a greater extent and is longer lived in the process catalyzed by the A69L mutant637493
A69LEscherichia coli-the small side chain of Ala-69 is required for rapid elongation to the C55 product637493
C234AEscherichia coli-kinetik data similar to wild-type. Crystallization data699031
D150AEscherichia coli-turnover-number is 44% of the activity of the wild-type enzyme, Km value for (2E,6E)-farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 50fold higher than that of the wild-type enzyme; turnover-number is 44% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 50fold higher than that of the wild-type enzyme637495
D190AEscherichia coli-no significant change637495
D218AEscherichia coli-turnover-number is about 9% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme637495
D223AEscherichia coli-no significant change637495
D26AEscherichia coli-turnover-number is less than 1% of that of the wild-type enzyme, Km value for farnesyl diphosphate is comparable to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 3.5fold higher than that of the wild-type enzyme637495
D26AEscherichia coli-site-directed mutagenesis, reduced activity compared to the wild-type enzyme659232
D26AEscherichia coli-site-directed mutagenesis, altered Mg2+ binding and about 1000fold reduced activity compared to the wild-type enzyme; site-directed mutagenesis, altered Mg2+ binding and about 1000fold reduced activity compared to the wild-type enzyme659476
D26EEscherichia coli-site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme; site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme659476
D26KEscherichia coli-site-directed mutagenesis, altered Mg2+ binding and about 10000fold reduced activity compared to the wild-type enzyme; site-directed mutagenesis, altered Mg2+ binding and about 10000fold reduced activity compared to the wild-type enzyme659476
D26REscherichia coli-site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme; site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme659476
DELTAS72Escherichia coli-loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs707467
DELTAS83Escherichia coli-loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs707467
DELTAV82S83Escherichia coli-loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs707467
E198AEscherichia coli-no significant change637495
E213AEscherichia coli-turnover-number is less than 1% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is 1.75fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 68.3fold higher than that of the wild-type enzyme637495
E213AEscherichia coli-site-directed mutagenesis, reduced activity compared to the wild-type enzyme659232
E73AEscherichia coli-turnover-number is 12% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 3.9fold higher than that of the wild-type enzyme637493
E73AEscherichia coli-turnover-number is 12% of that of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 4fold higher than that of the wild-type enzyme637495
E81AEscherichia coli-increases in the IPP Km values; turnover-number is 16% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 21.5fold higher than that of the wild-type enzyme637493
F89AEscherichia coli-mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity; site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme657857
H103AEscherichia coli-the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs637493
H199AEscherichia coli-site-directed mutagenesis, activity is similar to the wild-type enzyme659232
H199A/E213AEscherichia coli-site-directed mutagenesis, reduced activity compared to the wild-type enzyme659232
H43AEscherichia coli-site-directed mutagenesis, reduced activity compared to the wild-type enzyme659232
I62AEscherichia coli-the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs637493
L137AEscherichia coli-catalysis results in predominantly the formation of the C70 polymer rather than the C55 polymer; mutant enzyme produces C55-polyprenyl diphosphate, C60-polyprenyl diphosphate and C65-polyprenyl diphosphate in the ratio 55:41:4 in presence of Triton, compared to the wild-type enzyme which produces C55-polyprenyl diphosphate as the major product. In absence of Triton the mutant enzyme produces C70 and C75-polyprenyl diphosphate is the major products637493
L85AEscherichia coli-mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity; site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme657857
N74AEscherichia coli-decrease in kcat values; turnover-number is less than 1% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 2fold higher than that of the wild-type enzyme637493
R77AEscherichia coli-decrease in kcat values; turnover-number is less than 1% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 4fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 3.8fold higher than that of the wild-type enzyme637493
S71AEscherichia coli-decrease in kcat values; increases in the IPP Km values; turnover-number is 4.4% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 2.5fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 32.4fold higher than that of the wild-type enzyme637493
S83(Ala)1Escherichia coli-mutant with amino acids inserted into the loop707467
S83(Ala)5Escherichia coli-mutant with amino acids inserted into the loop707467
V105AEscherichia coli-the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs637493
W149FEscherichia coli-turnover-number is 68% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 1.75fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 4.9fold higher than that of the wild-type enzyme637494
W207FEscherichia coli-turnover-number is 60% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 8.5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 5.6fold higher than that of the wild-type enzyme637494
W221FEscherichia coli-turnover-number is 140% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 1.3fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 3.4fold higher than that of the wild-type enzyme637494
W31FEscherichia coli-turnover-number is 44% of that of the wild-type enzyme,Km-value for farnesyl diphosphate is 5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 1.4fold higher than that of the wild-type enzyme637494
W75AEscherichia coli-shows 8fold increase of the FPP Km value; turnover-number is 4.4% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 8fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 11.2fold higher than that of the wild-type enzyme637493
W75FEscherichia coli-turnover-number is 44% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 4.5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme637494
W91FEscherichia coli-turnover-number is equal to that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 1.8fold higher than that of the wild-type enzyme637494
C234AHelicobacter pyloriP55984kinetic data similar to wild-type. Crystallization data; site-directed mutagenesis, mutation to prevent intramolecular disulfide bond formed during the long period of crystallization process699031
C234AHelicobacter pylori-C234A UPPS mutant is crystallized using the hanging drop method, C234A has unchanged kinetic properties compared to wild-type704720
A72LMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
A72L/F73LMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
A72L/F73L/W78LMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
D221AMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity637491
D226AMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity637491
D29AMicrococcus luteus-Km-value for farnesyl diphosphate is 9.2fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 5.8fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 1% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 9.2fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 5.8fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 1% of that of the wild-type enzyme637492
E193QMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity637491
E201QMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity637491
E216QMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 11.6fold higher than that for the wild-type enzyme, turnover number is about 18fold lower. The major products contain C35 and C50 prenyl chain length; site-directed mutagenesis, Km value increased637491
E76QMicrococcus luteus-Km-value for farnesyl diphosphate is 1.6fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 3.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.5fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 30% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 1.6fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 3.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.5fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 30% of that of the wild-type enzyme637492
E84QMicrococcus luteus-Km-value for farnesyl diphosphate is 3.2fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.98fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 65% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 3.2fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.98fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 65% of that of the wild-type enzyme637492
F207SMicrococcus luteus-site-directed mutagenesis, reduced activity, and 13fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme; site-directed mutagenesis, reduced activity, and 13fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme659084
F223HMicrococcus luteus-dramatically decreased catalytic activity when farnesyl diphosphate is used as allylic substrate673574
F227SMicrococcus luteus-site-directed mutagenesis659084
F73AMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. 32fold increase in Km-value for isopentenyl diphosphate and about 17fold decrease in turnover-number. A mixture of C30 and C50 products is formed; yielded shorter chain prenyl diphosphates as their main products637491
F73AMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
F73LMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
G32RMicrococcus luteus-Km-value for farnesyl diphosphate is comparable to that of the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.9fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 27% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is comparable to that of the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.9fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 27% of that of the wild-type enzyme637492
G32R/R42GMicrococcus luteus-Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.4fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 58% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.4fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 58% of that of the wild-type enzyme637492
N77AMicrococcus luteus-dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type637487
N77DMicrococcus luteus-dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type637487
N77QMicrococcus luteus-dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type637487
R197SMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 7.2fold higher than that for the wild-type enzyme, turnover-number is 1200fold lower. Compared with the wild-type enzyme lower reaction rate in catalysis and fewer product produced after 6 h reaction; site-directed mutagenesis, Km value increased637491
R203SMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 8fold higher than that for the wild-type enzyme, turnover-number is 1200fold lower. Compared with the wild-type enzyme lower reaction rate in catalysis and fewer product produced after 6 h reaction; site-directed mutagenesis, Km value increased637491
R33AMicrococcus luteus-Km-value for farnesyl diphosphate is 40fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.2fold lower than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 3% of that of the wild-type enzyme. Different product distribution pattern compared to the wildf-type enzyme; Km-value for farnesyl diphosphate is 40fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.2fold lower than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 3% of that of the wild-type enzyme. Different product distribution pattern compared to the wildf-type enzyme637492
R42GMicrococcus luteus-Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.8fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.1fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 13% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.8fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.1fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 13% of that of the wild-type enzyme637492
R80AMicrococcus luteus-Km-value for farnesyl diphosphate is 6.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is less than 1% of that of the wild-type enzyme; Km-value for farnesyl diphosphate is 6.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is less than 1% of that of the wild-type enzyme637492
S74AMicrococcus luteus-comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. 16fold increase in Km-value for isopentenyl diphosphate and about 12fold decrease in turnover-number. The major products contain C35 and C50 prenyl chain length; yielded shorter chain prenyl diphosphates as their main products637491
W210AMicrococcus luteus-site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme; site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme659084
W224AMicrococcus luteus-site-directed mutagenesis, reduced activity, 6fold increased Km for farnesyl diphosphate, and 14fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme; site-directed mutagenesis, reduced activity, 6fold increased Km for farnesyl diphosphate, and 14fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme659084
W78DMicrococcus luteus-moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 18.7fold increase in Km-value for farnesyl diphosphate637487
W78IMicrococcus luteus-moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 6-fold increase in Km-value for farnesyl diphosphate, 2.3fold increase in Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate; moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 6-fold increase in Km-value for farnesyl diphosphate, 2.3fold increase in Km-value for (Z,E,E)-geranylgeranyl diphosphate637487
W78LMicrococcus luteus-mutation results in shorter ultimate products with C20-35673574
W78RMicrococcus luteus-moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 14.5-fold increase in Km-value for farnesyl diphosphate, 1.8fold increase in Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate; moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 14.5-fold increase in Km-value for farnesyl diphosphate, 1.8fold increase in Km-value for (Z,E,E)-geranylgeranyl diphosphate637487
Y148FMicrococcus luteus-site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme; site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme659084
Y148SMicrococcus luteus-site-directed mutagenesis, inactive mutant; site-directed mutagenesis, inactive mutant659084
L88AEscherichia coli-mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity; site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme657857
additional informationEscherichia coli-loop-shortening mutants with deletion of V82 and S83 or S72 also adopt an open conformation with the loop stretched, although they show decreased intrinsic fluorescence with (2E,6E)-farnesyl diphosphate bound, similar to that seen in the wild-type enzyme707467
Y71SMicrococcus luteus-site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme; site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme659084
additional informationStreptococcus pneumoniae R6-four uppS deletion mutants of Streptococcus pneumoniae R6 pKO1-4708911

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
the recombinant protein in the pellet is solubilized with 7 M urea and purified using nickel-nitrilotriacetic acid under denaturing conditions. The protein refolding is achieved via the stepwise dialysis to remove the denaturant in the presence of 6 mM beta-mercaptoethanol. Alternatively, on-column refolding is carried out in a single step to obtain the active protein in large quantities. beta-Mercaptoethanol and Triton are both required in this quick refolding processSaccharomyces cerevisiae-637486

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
medicineHelicobacter pyloriP55984enzyme represents a potential target for developing new antibiotics699031

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
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637481Baba, T.; Allen, C.M.Prenyl transferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetaseArch. Biochem. Biophys.200474-4841980Micrococcus luteus PubMed
637482Fujisaki, S.; Nishino, T.; Katasuki, H.Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesisJ. Biochem.991327-13371986Escherichia coli PubMed
637483Baba, T.; Allen, C.M.Substrate specificity of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarumBiochemistry175598-56041978Lactobacillus plantarum PubMed
637484Allen, C.M.; Muth, J.D.Lipid activation of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarumBiochemistry162908-29151977Lactobacillus plantarum PubMed
637485Pan, J.J.; Chiou, S.T.; Liang, P.H.Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reactionBiochemistry3910936-109422000Escherichia coli PubMed
637486Chang, S.Y.; Tsai, P.C.; Tseng, C.S.; Liang, P.H.Refolding and characterization of a yeast dehydrodolichyl diphosphate synthase overexpressed in Escherichia coliProtein Expr. Purif.23432-4392001Saccharomyces cerevisiae PubMed
637487Fujikura, K.; Zhang, Y.W.; Yoshizaki, H.; Nishino, T.; Koyama, T.Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26J. Biochem.128917-9222000Micrococcus luteus PubMed
637488Shimizu, N.; Koyama, T.; Ogura, K.Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthasesJ. Biol. Chem.27319476-194811998Escherichia coli, Micrococcus luteus PubMed
637489Fujihashi, M.; Zhang, Y.W.; Higuchi, Y.; Li, X.Y.; Koyama, T.; Miki, K.Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthaseProc. Natl. Acad. Sci. USA984337-43422001Micrococcus luteus PubMed
637491Kharel, Y.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.Identification of significant residues for homoallylic substrate binding of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthaseJ. Biol. Chem.27628459-284642001Micrococcus luteus PubMed
637492Fujikura, K.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthaseBiochemistry424035-40412003Micrococcus luteus PubMed
637493Ko, T.P.; Chen, Y.K.; Robinson, H.; Tsai, P.C.; Gao, Y.G.; Chen, A.P.C.; Wang, A.H.J.; Liang, P.H.Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysisJ. Biol. Chem.27647474-474822001Escherichia coli PubMed
637494Chen, Y.H.; Chen, A.P.C.; Chen, C.T.; Wang, A.H.J.; Liang, P.H.Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutantsJ. Biol. Chem.2777369-73762002Escherichia coli PubMed
637495Pan, J.J.; Yang, L.W.; Liang, P.H.Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysisBiochemistry3913856-138612000Escherichia coli PubMed
657857Chen, A.P.; Chang, S.Y.; Lin, Y.C.; Sun, Y.S.; Chen, C.T.; Wang, A.H.; Liang, P.H.Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthaseBiochem. J.386169-1762005Escherichia coli PubMed
659084Khare, Y.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthaseJ. Biochem.134819-8262003Micrococcus luteus PubMed
659232Chang, S.Y.; Ko, T.P.; Liang, P.H.; Wang, A.H.Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and tritonJ. Biol. Chem.27829298-293072003Escherichia coli PubMed
659476Guo, R.T.; Ko, T.P.; Chen, A.P.; Kuo, C.J.; Wang, A.H.; Liang, P.H.Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysisJ. Biol. Chem.28020762-207742005Escherichia coli PubMed
660464Chang, S.Y.; Ko, T.P.; Chen, A.P.; Wang, A.H.; Liang, P.H.Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studiesProtein Sci.13971-9782004Escherichia coli PubMed
673055Takahashi, S.; Koyama, T.Structure and function of cis-prenyl chain elongating enzymesChem. Rec.6194-2052006Escherichia coli, Micrococcus luteus PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.31)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)