Ligand spermine

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Basic Ligand Information

Molecular Structure
Picture of spermine (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C10H26N4
spermine
PFNFFQXMRSDOHW-UHFFFAOYSA-N
Synonyms:
H2N(CH2)3NH(CH2)4NH(CH2)3NH2, N,N'-bis(3-aminopropyl)-1,4-butanediamine, N,N'-bis(3-aminopropyl)tetramethylenediamine, spermine[side 2]


Show all pahtways known for Show all BRENDA pathways known for spermine

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
spermine + H2O + O2 = ?
show the reaction diagram
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spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
show the reaction diagram
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spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2
show the reaction diagram
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putrescine + spermine = sym-homospermine + propane-1,3-diamine
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
N1-acetylspermine + H2O = acetate + spermine
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (45 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
spermine + O2 + H2O = N,N'-bis(3-aminopropyl)-4-aminobutanal + NH3 + H2O2
show the reaction diagram
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spermine + O2 + H2O = ?
show the reaction diagram
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spermine + H2O + 2,6-dichlorophenol indophenol = ? + NH3 + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
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carbamoyl phosphate + spermine = phosphate + N-carbamoylspermine
show the reaction diagram
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acetyl-CoA + spermine = ?
show the reaction diagram
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S-adenosyl 3-(methylthio)propylamine + spermine = S-methyl-5'-thioadenosine + N4-aminopropylspermine
show the reaction diagram
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putrescine + spermine = sym-homospermine + propane-1,3-diamine
show the reaction diagram
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[eIF5A-precursor]-lysine + spermine = ?
show the reaction diagram
spermine + pyruvate = ? + L-alanine
show the reaction diagram
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spermine/out + ATP + H2O = spermine/in + ADP + phosphate
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
N-(3-aminopropyl)-N-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O = spermine + H2O2 + ?
show the reaction diagram
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S-adenosylmethioninamine + spermidine = 5'-S-methyl-5'-thioadenosine + spermine
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (90 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulates in vitro
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in the absence of exogenous Ca2+ and Mg2+ and in the presence of EGTA, which favours the release of endogenous Ca2+, spermine is able to stimulate the activity of pyruvate dehydrogenase complex (maximum stimulation of about 140% at 0.5 mM after 30 min of incubation, at concentrations higher than 0.5 mM, spermine still stimulates PDC, when compared with the control, but shows a slight dose-dependent decrease). The interaction of spermine with PDC may also involve activation of pyruvate dehydrogenase kinase, resulting in an increase in E1alpha phosphorylation and consequently reduced stimulation of PDC at high polyamine concentrations
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enhances activity
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13% activation at 1.2 mM
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1 mM, stimulation
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activation
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up to 4 fold stimulation at 1 mm
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activates at 1 mM
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activation, 5 mM
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slight activation
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activates about 3fold in presence of 0.1 mg/ml bovine serum albumin
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activates acetylation of H3
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0.07 mM spermine treatment significantly increases the enzyme activity at 15 and 35 days after post anthesis
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stimulate
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activator
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increases activity
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aliphatic, positively charged polyamine, required for in vitro activity of ORF47, polyamine depletion leads to 80% reduced activity
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at low concentrations: up to 20% activation, inhibits at higher concentrations
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PLC d1 and PLC d3
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stimulates activity
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maximal stimulation at 0.06 mM
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interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation. Spermine interacts with proteinase K spontaneously at single binding site
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1 mM, enhances arginase activity by 33%
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at concentration of 0.1 g/l about 2% more putrescine production, at concentration of 1 g/l 23% more putrescine production
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or spermidine required, enhances extent and accuracy of cleavage, degree of stimulation varies with the pre-tRNA substrate
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enhances activity against poly(C) and yeast RNA, reverses inhibition by poly(G) by removal of inhibitor from the enzymes surface
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slight stimulation, additionally spermine increases the enzyme activity by stabilizing conformation of negatively charged DNA
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supports aminoacylation in presence of crude tRNA not in presence of resolved tRNA
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stimulates only at low Mg2+ concentrations
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chloroplastic enzyme: unable to promote aminoacylation in absence of Mg2+. In presence of suboptimal concentrations of Mg2+, spermine can restore maximal activity (not in cytoplasmic enzyme)
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stimulates activity only in absence of NH4+
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0.5 mM, increases the Km for nicked DNA, increases reaction velocity
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Inhibitor in Enzyme-catalyzed Reactions (82 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
41% of initial activity at 0.5 mM
-
competitive inhibition of putrescine oxidation
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12 mM
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weak inhibitor at pH 8.0
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the early decrease of glutathione reductase activity in leaves treated with polyamines can be due to a direct interaction of these compounds with the enzyme
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1 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate
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inhibits slightly in absence of bovine serum albumin
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competitive to L-arginyl-tRNA
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99% inhibition at 0.1 mM and 90% inhibition at 1 mM
mixed type inhibition
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30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM; 30-40% inhibition with 5 mM
-
weak
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0.03 mg/ml, 50% inhibition
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1 mM enhances activity 3times, inhibition above 1 mM
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bovine serum albumin, not protamine as substrate
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at higher concentrations, activates at low concentrations
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slight inhibition of poly(U)-degradation
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inhibition of Mn2+-dependent enzyme, no inhibition of the Mg2+-dependent enzyme
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2.0-20 mM
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70% inhibition at 0.1 mM
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above 0.06 mM
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at 0.13 mM: inhibition, at 0.02 M: activity towards cyclic substrates and poly(C) is activated, not towards poly(U)
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catalyzes ATP-diphosphate exchange, no inhibition of specific aminoacylation of tRNAIle
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strongly inhibits the ATPase activity of PotA
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Metals and Ions (2 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates, can partially replace Mg2+
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optimal at 1 mM, stimulates 2-4fold the second reaction step, the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
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3D Structure of Enzyme-Ligand-Complex (PDB) (87 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (68 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.18
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

KM Value (103 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.47
-
wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C
0.698
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at pH 7.0 and 37°C
0.35
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Ki Value (14 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.25
-
competitive inhibition
0.0581
-
-
0.75
-
-
200
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at pH 8.0
3.2
-
-
0.0008
-
-
0.0022
-
-
17
-
pH 8.0, 37°C
1.15
-
-
10
-
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IC50 Value (4 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
1.6
-
IC50: 1.6 mM

References & Links

Links to other databases for spermine

ChEBI
PubChem
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PubChem