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Your query returned 37 entries. Printable version
EC | 1.4.3.4 | ||||||||||||||||||
Accepted name: | monoamine oxidase | ||||||||||||||||||
Reaction: | RCH2NHR′ + H2O + O2 = RCHO + R′NH2 + H2O2 | ||||||||||||||||||
Other name(s): | adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; MAO; MAO A; MAO B; MAO-A; MAO-B; monoamine oxidase A; monoamine oxidase B; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase | ||||||||||||||||||
Systematic name: | amine:oxygen oxidoreductase (deaminating) | ||||||||||||||||||
Comments: | A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide. | ||||||||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-66-5 | ||||||||||||||||||
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EC | 1.4.3.27 | ||||||||||||||||||
Accepted name: | homospermidine oxidase | ||||||||||||||||||
Reaction: | sym-homospermidine + 2 O2 + H2O = 1-formylpyrrolizidine + 2 H2O2 + 2 NH3 (overall reaction) (1a) sym-homospermidine + O2 = N-(4-aminobutylpyrrolinium) ion + H2O2 + NH3 (1b) N-(4-aminobutylpyrrolinium) ion + O2 + H2O = N-(4-oxobutylpyrrolinium) ion + NH3 + H2O2 (1c) N-(4-oxobutylpyrrolinium) ion = 1-formylpyrrolizidine (spontaneous) |
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Glossary: | (–)-trachelanthamidine = (1R,7aS)-hexahydro-1H-pyrrolizin-1-ylmethanol | ||||||||||||||||||
Other name(s): | HSO | ||||||||||||||||||
Systematic name: | homospermidine:oxygen oxidase (deaminating, cyclizing) | ||||||||||||||||||
Comments: | The copper-containing enzyme has been isolated from the plant Heliotropium indicum. It is involved in the biosynthesis of the pyrrolizidine alkaloid (–)-trachelanthamidine which acts as a secondary metabolite for the defense against herbivores. The oxidation of sym-homospermidine proceeds in three steps and results in a cyclization. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 1.5.1.43 | ||||||||||||||||||
Accepted name: | carboxynorspermidine synthase | ||||||||||||||||||
Reaction: | (1) carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ (2) carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+ |
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Other name(s): | carboxynorspermidine dehydrogenase; carboxyspermidine dehydrogenase; CASDH; CANSDH; VC1624 (gene name) | ||||||||||||||||||
Systematic name: | carboxynorspermidine:NADP+ oxidoreductase | ||||||||||||||||||
Comments: | The reaction takes place in the opposite direction. Part of a bacterial polyamine biosynthesis pathway. L-aspartate 4-semialdehyde and propane-1,3-diamine/putrescine form a Schiff base that is reduced to form carboxynorspermidine/carboxyspermidine, respectively [1]. The enzyme from the bacterium Vibrio cholerae is essential for biofilm formation [2]. The enzyme from Campylobacter jejuni only produces carboxyspermidine in vivo even though it also can produce carboxynorspermidine in vitro [3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 1.5.3.11 | ||||||||||||||||||
Deleted entry: | polyamine oxidase. Now included with EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase) | ||||||||||||||||||
EC | 1.5.3.13 | ||||||||||||||||||
Accepted name: | N1-acetylpolyamine oxidase | ||||||||||||||||||
Reaction: | (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 (2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 |
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Other name(s): | hPAO-1; PAO (ambiguous); mPAO; hPAO; polyamine oxidase (ambiguous) | ||||||||||||||||||
Systematic name: | N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming) | ||||||||||||||||||
Comments: | The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 1.5.3.14 | ||||||||||||||||||
Accepted name: | polyamine oxidase (propane-1,3-diamine-forming) | ||||||||||||||||||
Reaction: | spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal + H2O2 | ||||||||||||||||||
Other name(s): | MPAO (ambiguous); maize PAO | ||||||||||||||||||
Systematic name: | spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) | ||||||||||||||||||
Comments: | As the products of the reaction cannot be converted directly to other polyamines, this class of polyamine oxidases is considered to be involved in the terminal catabolism of polyamines [1]. This enzyme less efficiently catalyses the oxidation of N1-acetylspermine and spermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 1.5.3.15 | ||||||||||||||||||
Accepted name: | N8-acetylspermidine oxidase (propane-1,3-diamine-forming) | ||||||||||||||||||
Reaction: | N8-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2 | ||||||||||||||||||
Systematic name: | N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) | ||||||||||||||||||
Comments: | Also active with N1-acetylspermine, weak activity with N1,N12-diacetylspermine. No activity with diaminopropane, putrescine, cadaverine, diaminohexane, norspermidine, spermine and spermidine. Absence of monoamine oxidase (EC 1.4.3.4) activity. Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 1.5.3.16 | ||||||||||||||||||
Accepted name: | spermine oxidase | ||||||||||||||||||
Reaction: | spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2 | ||||||||||||||||||
Other name(s): | PAOh1/SMO; PAOh1 (ambiguous); AtPAO1; AtPAO4; SMO; mSMO; SMO(PAOh1); SMO/PAOh1; SMO5; mSMOmu | ||||||||||||||||||
Systematic name: | spermidine:oxygen oxidoreductase (spermidine-forming) | ||||||||||||||||||
Comments: | The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N1-acetylspermine. A flavoprotein (FAD). Differs in specificity from EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming) and EC 1.5.3.17 (non-specific polyamine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 1.5.3.17 | ||||||||||||||||||
Accepted name: | non-specific polyamine oxidase | ||||||||||||||||||
Reaction: | (1) spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2 (2) spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 (3) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 (4) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 |
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Other name(s): | polyamine oxidase (ambiguous); Fms1; AtPAO3 | ||||||||||||||||||
Systematic name: | polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming) | ||||||||||||||||||
Comments: | A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 1.5.99.6 | ||||||||||||||||||
Accepted name: | spermidine dehydrogenase | ||||||||||||||||||
Reaction: | spermidine + acceptor + H2O = propane-1,3-diamine + 4-aminobutanal + reduced acceptor | ||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine | ||||||||||||||||||
Other name(s): | spermidine:(acceptor) oxidoreductase | ||||||||||||||||||
Systematic name: | spermidine:acceptor oxidoreductase | ||||||||||||||||||
Comments: | A flavohemoprotein (FAD). Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as acceptor. 4-Aminobutanal condenses non-enzymically to 1-pyrroline. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-64-6 | ||||||||||||||||||
References: |
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EC | 1.8.1.12 | ||||||||||||||||||
Accepted name: | trypanothione-disulfide reductase | ||||||||||||||||||
Reaction: | trypanothione + NADP+ = trypanothione disulfide + NADPH + H+ | ||||||||||||||||||
For diagram of trypanothione biosynthesis, click here | |||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine trypanothione = N1,N8-bis(glutathionyl)spermidine |
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Other name(s): | trypanothione reductase; NADPH2:trypanothione oxidoreductase | ||||||||||||||||||
Systematic name: | trypanothione:NADP+ oxidoreductase | ||||||||||||||||||
Comments: | Trypanothione disulfide is the oxidized form of N1,N8-bis(glutathionyl)-spermidine from the insect-parasitic trypanosomatid Crithidia fasciculata. The enzyme from Crithidia fasciculata is a flavoprotein (FAD), whose activity is dependent on a redox-active cystine at the active centre. (cf. EC 1.8.1.7, glutathione-disulfide reductase) | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102210-35-5 | ||||||||||||||||||
References: |
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EC | 2.3.1.57 | ||||||||||||||||||
Accepted name: | diamine N-acetyltransferase | ||||||||||||||||||
Reaction: | acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine | ||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine |
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Other name(s): | spermidine acetyltransferase; putrescine acetyltransferase; putrescine (diamine)-acetylating enzyme; diamine acetyltransferase; spermidine/spermine N1-acetyltransferase; spermidine N1-acetyltransferase; acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase; putrescine acetylase; putrescine N-acetyltransferase | ||||||||||||||||||
Systematic name: | acetyl-CoA:alkane-α,ω-diamine N-acetyltransferase | ||||||||||||||||||
Comments: | Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54596-36-0 | ||||||||||||||||||
References: |
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EC | 2.3.1.248 | ||||||||||||||||||
Accepted name: | spermidine disinapoyl transferase | ||||||||||||||||||
Reaction: | 2 sinapoyl-CoA + spermidine = 2 CoA + N1,N8-bis(sinapoyl)-spermidine | ||||||||||||||||||
Other name(s): | SDT | ||||||||||||||||||
Systematic name: | sinapoyl-CoA:spermidine N-(hydroxycinnamoyl)transferase | ||||||||||||||||||
Comments: | The enzyme from the plant Arabidopsis thaliana has no activity with 4-coumaroyl-CoA (cf. EC 2.3.1.249, spermidine dicoumaroyl transferase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
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EC | 2.3.1.249 | ||||||||||||||||||
Accepted name: | spermidine dicoumaroyl transferase | ||||||||||||||||||
Reaction: | 2 4-coumaroyl-CoA + spermidine = 2 CoA + N1,N8-bis(4-coumaroyl)-spermidine | ||||||||||||||||||
Other name(s): | SCT | ||||||||||||||||||
Systematic name: | 4-coumaroyl-CoA:spermidine N-(hydroxycinnamoyl)transferase | ||||||||||||||||||
Comments: | The enzyme from the plant Arabidopsis thaliana has no activity with sinapoyl-CoA (cf. EC 2.3.1.248, spermidine disinapoyl transferase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 2.5.1.16 | ||||||||||||||||||
Accepted name: | spermidine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5′-thioadenosine + spermidine | ||||||||||||||||||
For diagram of spermine biosynthesis, click here | |||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine putrescine = butane-1,4-diamine S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium |
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Other name(s): | aminopropyltransferase; putrescine aminopropyltransferase; spermidine synthetase; SpeE (ambiguous); S-adenosylmethioninamine:putrescine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:putrescine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-82-0 | ||||||||||||||||||
References: |
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EC | 2.5.1.22 | ||||||||||||||||||
Accepted name: | spermine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + spermine | ||||||||||||||||||
For diagram of spermine biosynthesis, click here | |||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium |
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Other name(s): | spermidine aminopropyltransferase; spermine synthetase; S-adenosylmethioninamine:spermidine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme from mammalia is highly specific for spermidine [2,3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.23 (sym-norspermidine synthase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74812-43-4 | ||||||||||||||||||
References: |
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EC | 2.5.1.23 | ||||||||||||||||||
Accepted name: | sym-norspermidine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + propane-1,3-diamine = S-methyl-5′-thioadenosine + bis(3-aminopropyl)amine | ||||||||||||||||||
Glossary: | S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium | ||||||||||||||||||
Other name(s): | S-adenosylmethioninamine:propane-1,3-diamine 3-aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:propane-1,3-diamine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:propane-1,3-diamine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme has been originally characterized from the protist Euglena gracilis [1,2]. The enzyme from the archaeon Sulfolobus solfataricus can transfer the propylamine moiety from S-adenosyl 3-(methylsulfanyl)propylamine to putrescine, sym-norspermidine and spermidine with lower efficiency [3]. cf. EC 2.5.1.16 (spermidine synthase) and EC 2.5.1.22 (spermine synthase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 2.5.1.44 | ||||||||||||||||||
Accepted name: | homospermidine synthase | ||||||||||||||||||
Reaction: | (1) 2 putrescine = sym-homospermidine + NH3 (2) spermidine + putrescine = sym-homospermidine + propane-1,3-diamine |
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For diagram of reaction, click here | |||||||||||||||||||
Glossary: | sym-homospermidine = N1-(4-aminobutyl)butane-1,4-diamine putrescine = butane-1,4-diamine |
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Other name(s): | putrescine:putrescine 4-aminobutyltransferase (ammonia-forming) | ||||||||||||||||||
Systematic name: | putrescine/spermidine:putrescine 4-aminobutyltransferase | ||||||||||||||||||
Comments: | The reaction of this bacterial enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (a) NAD+-dependent dehydrogenation of either putrescine or spermidine, forming 4-iminobutan-1-amine or (E)-(4-aminobutylidene)(3-aminopropyl)amine, respectively, (b) attack by water forming 4-aminobutanal (and releasing ammonia or propane-1,3-diamine, respectively), and (c) condensation of 4-aminobutanal with putrescine, which forms homospermidine and restores NAD+. Differs from the eukaryotic enzyme EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 76106-84-8 | ||||||||||||||||||
References: |
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EC | 2.5.1.45 | ||||||||||||||||||
Accepted name: | homospermidine synthase (spermidine-specific) | ||||||||||||||||||
Reaction: | spermidine + putrescine = sym-homospermidine + propane-1,3-diamine | ||||||||||||||||||
For diagram of reaction, click here | |||||||||||||||||||
Glossary: | sym-homospermidine = N1-(4-aminobutyl)butane-1,4-diamine putrescine = butane-1,4-diamine spermidine.html">spermidine = N1-(3-aminopropyl)butane-1,4-diamine |
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Systematic name: | spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming) | ||||||||||||||||||
Comments: | A eukaryotic enzyme found in plants. The reaction occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: (a) NAD+-dependent dehydrogenation of spermidine to 4-iminobutan-1-amine, (b) attack by water forming 4-aminobutanal (and releasing propane-1,3-diamine), and (c) condensation of 4-aminobutanal with purescine, which forms homospermidine and restores NAD+. This enzyme is more specific than EC 2.5.1.44, homospermidine synthase, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 2.5.1.46 | ||||||||||||||||||
Accepted name: | deoxyhypusine synthase | ||||||||||||||||||
Reaction: | [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction) (1a) spermidine + NAD+ = dehydrospermidine + NADH (1b) dehydrospermidine + [enzyme]-lysine = N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine (1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine = N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine (1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ = [eIF5A-precursor]-deoxyhypusine + NAD+ |
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For diagram of reaction, click here | |||||||||||||||||||
Glossary: | deoxyhypusine = N6-(4-aminobutyl)-L-lysine hypusine = N6-[(R)-4-amino-2-hydroxybutyl]-L-lysine spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine |
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Other name(s): | spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming) | ||||||||||||||||||
Systematic name: | [eIF5A-precursor]-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming) | ||||||||||||||||||
Comments: | The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. The reaction occurs in four steps: NAD+-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme; 1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29, deoxyhypusine monooxygenase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 127069-31-2 | ||||||||||||||||||
References: |
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EC | 2.5.1.79 | ||||||||||||||||||
Accepted name: | thermospermine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + thermospermine + H+ | ||||||||||||||||||
Glossary: | thermospermine = N1-[3-(3-aminopropylamino)propyl]butane-1,4-diamine S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium |
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Other name(s): | TSPMS; ACL5; SAC51; S-adenosyl 3-(methylthio)propylamine:spermidine 3-aminopropyltransferase (thermospermine synthesizing) | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase (thermospermine-forming) | ||||||||||||||||||
Comments: | This plant enzyme is crucial for the proper functioning of xylem vessel elements in the vascular tissues of plants [3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 2.5.1.104 | ||||||||||||||||||
Accepted name: | N1-aminopropylagmatine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + agmatine = S-methyl-5′-thioadenosine + N1-(3-aminopropyl)agmatine | ||||||||||||||||||
For diagram of spermidine biosynthesis, click here | |||||||||||||||||||
Glossary: | S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium | ||||||||||||||||||
Other name(s): | agmatine/cadaverine aminopropyl transferase; ACAPT; PF0127 (gene name); triamine/agmatine aminopropyltransferase; SpeE (ambiguous); agmatine aminopropyltransferase; S-adenosyl 3-(methylthio)propylamine:agmatine 3-aminopropyltransferase | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:agmatine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. cf. EC 2.5.1.16, spermidine synthase, and EC 2.5.1.23, sym-norspermidine synthase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 2.5.1.126 | ||||||||||||||||||
Accepted name: | norspermine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + norspermidine = S-methyl-5′-thioadenosine + norspermine | ||||||||||||||||||
Glossary: | norspermidine = bis(3-aminopropyl)amine norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine spermidine = N-(3-aminopropyl)-1,4-butanediamine thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine |
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Other name(s): | long-chain polyamine synthase (ambiguous) | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:norspermidine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 2.5.1.127 | ||||||||||||||||||
Accepted name: | caldopentamine synthase | ||||||||||||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + norspermine = S-methyl-5′-thioadenosine + caldopentamine | ||||||||||||||||||
Glossary: | caldopentamine = N-(3-aminopropyl)-N′-{3-[(3-aminopropyl)amino]propyl}-1,3-propanediamine norspermidine = N-(3-aminopropyl)-1,4-butanediamine norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine spermidine = N-(3-aminopropyl)-1,4-butanediamine thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine |
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Other name(s): | long-chain polyamine synthase (ambiguous) | ||||||||||||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:norspermine 3-aminopropyltransferase | ||||||||||||||||||
Comments: | The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 2.5.1.128 | ||||||||||||||||||
Accepted name: | N4-bis(aminopropyl)spermidine synthase | ||||||||||||||||||
Reaction: | 2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2 S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine (overall reaction) (1a) S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = S-methyl-5′-thioadenosine + N4-aminopropylspermidine (1b) S-adenosyl 3-(methylsulfanyl)propylamine + N4-aminopropylspermidine = S-methyl-5′-thioadenosine + N4-bis(aminopropyl)spermidine |
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Glossary: | spermidine = N-(3-aminopropyl)butane-1,4-diamine N4-aminopropylspermidine = N,N′-bis(3-aminopropyl)butane-1,4-diamine N4-bis(aminopropyl)spermidine = N,N,N′-tris(3-aminopropyl)butane-1,4-diamine |
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Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:spermidine 3-aminopropyltransferase [N4-bis(aminopropyl)spermidine synthesizing] | ||||||||||||||||||
Comments: | The enzyme, characterized from the thermophilic archaeon Thermococcus kodakarensis, synthesizes the branched-chain polyamine N4-bis(aminopropyl)spermidine, which is required for cell growth at high-temperature. When spermine is used as substrate, the enzyme forms N4-aminopropylspermine. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 2.6.1.82 | ||||||||||||||||||
Accepted name: | putrescine—2-oxoglutarate transaminase | ||||||||||||||||||
Reaction: | putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate | ||||||||||||||||||
For diagram of arginine catabolism, click here | |||||||||||||||||||
Glossary: | putrescine = butane-1,4-diamine 1-pyrroline = 3,4-dihydro-2H-pyrrole |
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Other name(s): | putrescine-α-ketoglutarate transaminase; YgjG; putrescine:α-ketoglutarate aminotransferase; PAT (ambiguous); putrescine transaminase (ambiguous); putrescine aminotransferase (ambiguous); butane-1,4-diamine:2-oxoglutarate aminotransferase | ||||||||||||||||||
Systematic name: | putrescine:2-oxoglutarate aminotransferase | ||||||||||||||||||
Comments: | A pyridoxal 5′-phosphate protein [3]. The product, 4-aminobutanal, spontaneously cyclizes to form 1-pyrroline, which may be the actual substrate for EC 1.2.1.19, aminobutyraldehyde dehydrogenase. Cadaverine and spermidine can also act as substrates [3]. Forms part of the arginine-catabolism pathway [2]. cf. EC 2.6.1.113, putrescine—pyruvate transaminase. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 98982-73-1 | ||||||||||||||||||
References: |
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EC | 3.5.1.48 | ||||||||||||||||||
Accepted name: | acetylspermidine deacetylase | ||||||||||||||||||
Reaction: | N8-acetylspermidine + H2O = acetate + spermidine | ||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine |
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Other name(s): | N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect); 8-N-acetylspermidine amidohydrolase | ||||||||||||||||||
Systematic name: | N8-acetylspermidine amidohydrolase | ||||||||||||||||||
Comments: | It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction [1] but this has since been disproved by Marchant et al. [3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 67339-07-5 | ||||||||||||||||||
References: |
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EC | 3.5.1.62 | ||||||||||||||||||
Accepted name: | acetylputrescine deacetylase | ||||||||||||||||||
Reaction: | N-acetylputrescine + H2O = acetate + putrescine | ||||||||||||||||||
Glossary: | putrescine = butane-1,4-diamine spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine |
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Systematic name: | N-acetylputrescine acetylhydrolase | ||||||||||||||||||
Comments: | The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 103679-48-7 | ||||||||||||||||||
References: |
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EC | 3.5.1.63 | ||||||||||||||||||
Accepted name: | 4-acetamidobutyrate deacetylase | ||||||||||||||||||
Reaction: | 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate | ||||||||||||||||||
Glossary: | 4-aminobutanoate = γ-aminobutyrate = GABA | ||||||||||||||||||
Systematic name: | 4-acetamidobutanoate amidohydrolase | ||||||||||||||||||
Comments: | Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-82-0 | ||||||||||||||||||
References: |
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EC | 3.5.1.78 | ||||||||||||||||||
Accepted name: | glutathionylspermidine amidase | ||||||||||||||||||
Reaction: | glutathionylspermidine + H2O = glutathione + spermidine | ||||||||||||||||||
For diagram of trypanothione biosynthesis, click here | |||||||||||||||||||
Glossary: | spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine | ||||||||||||||||||
Other name(s): | glutathionylspermidine amidohydrolase (spermidine-forming) | ||||||||||||||||||
Systematic name: | γ-L-glutamyl-L-cysteinyl-glycine:spermidine amidase | ||||||||||||||||||
Comments: | Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 171040-71-4 | ||||||||||||||||||
References: |
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EC | 3.5.3.24 | ||||||||||||||||||
Accepted name: | N1-aminopropylagmatine ureohydrolase | ||||||||||||||||||
Reaction: | N1-(aminopropyl)agmatine + H2O = spermidine + urea | ||||||||||||||||||
For diagram of spermidine biosynthesis, click here | |||||||||||||||||||
Systematic name: | N1-(aminopropyl)agmatine amidinohydrolase | ||||||||||||||||||
Comments: | The enzyme, which has been characterized from the hyperthermophilic archaeon Pyrococcus kodakarensis and the thermophilic Gram-negative bacterium Thermus thermophilus, is involved in the biosynthesis of spermidine. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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EC | 3.6.3.31 | ||||||||||||||||||
Transferred entry: | polyamine-transporting ATPase. Now EC 7.6.2.11, polyamine-transporting ATPase | ||||||||||||||||||
EC | 4.1.1.50 | ||||||||||||||||||
Accepted name: | adenosylmethionine decarboxylase | ||||||||||||||||||
Reaction: | S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2 | ||||||||||||||||||
For diagram of spermidine biosynthesis, click here and for diagram of spermine biosynthesis, click here | |||||||||||||||||||
Glossary: | S-adenosyl 3-(methylsulfanyl)propylamine = (3-aminopropyl){[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}methylsulfonium | ||||||||||||||||||
Other name(s): | S-adenosylmethionine decarboxylase; S-adenosyl-L-methionine decarboxylase; S-adenosyl-L-methionine carboxy-lyase; S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming] | ||||||||||||||||||
Systematic name: | S-adenosyl-L-methionine carboxy-lyase [S-adenosyl 3-(methylsulfanyl)propylamine-forming] | ||||||||||||||||||
Comments: | The Escherichia coli enzyme contains a pyruvoyl group. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9036-20-8 | ||||||||||||||||||
References: |
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EC | 4.1.1.96 | ||||||||||||||||||
Accepted name: | carboxynorspermidine decarboxylase | ||||||||||||||||||
Reaction: | (1) carboxynorspermidine = bis(3-aminopropyl)amine + CO2 (2) carboxyspermidine = spermidine + CO2 |
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Glossary: | bis(3-aminopropyl)amine = norspermidine | ||||||||||||||||||
Other name(s): | carboxyspermidine decarboxylase; CANSDC; VC1623 (gene name) | ||||||||||||||||||
Systematic name: | carboxynorspermidine carboxy-lyase (bis(3-aminopropyl)amine-forming) | ||||||||||||||||||
Comments: | A pyridoxal 5′-phosphate enzyme. Part of a bacterial polyamine biosynthesis pathway. The enzyme is essential for biofilm formation in the bacterium Vibrio cholerae [1]. The enzyme from Campylobacter jejuni only produces spermidine in vivo even though it shows activity with carboxynorspermidine in vitro [3]. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||||
References: |
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EC | 6.3.1.8 | ||||||||||||||||||
Accepted name: | glutathionylspermidine synthase | ||||||||||||||||||
Reaction: | glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate | ||||||||||||||||||
For diagram of trypanothione biosynthesis, click here and for diagram of trypanothione biosynthesis, click here | |||||||||||||||||||
Glossary: | glutathione = γ-L-glutamyl-L-cysteinyl-glycine spermidine.html">spermidine = N-(3-aminopropyl)butane-1,4-diamine |
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Other name(s): | glutathione:spermidine ligase (ADP-forming) | ||||||||||||||||||
Systematic name: | γ-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP-forming) [spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule] | ||||||||||||||||||
Comments: | Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-09-2 | ||||||||||||||||||
References: |
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EC | 6.3.1.9 | ||||||||||||||||||
Accepted name: | trypanothione synthase | ||||||||||||||||||
Reaction: | (1) glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate (2) glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate |
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For diagram of trypanothione biosynthesis, click here and for diagram of trypanothione biosynthesis, click here | |||||||||||||||||||
Glossary: | N1,N8-bis(glutathionyl)spermidine = trypanothione | ||||||||||||||||||
Other name(s): | glutathionylspermidine:glutathione ligase (ADP-forming) | ||||||||||||||||||
Systematic name: | spermidine/glutathionylspermidine:glutathione ligase (ADP-forming) | ||||||||||||||||||
Comments: | The enzyme, characterized from several trypanosomatids (e.g. Trypanosoma cruzi) catalyses two subsequent reactions, leading to production of trypanothione from glutathione and spermidine. Some trypanosomatids (e.g. Crithidia species and some Leishmania species) also contain an enzyme that only carries out the first reaction (cf. EC 6.3.1.8, glutathionylspermidine synthase). The enzyme is bifunctional, and also catalyses the hydrolysis of glutathionylspermidine and trypanothione (cf. EC 3.5.1.78, glutathionylspermidine amidase). | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 130246-69-4 | ||||||||||||||||||
References: |
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EC | 7.6.2.11 | ||||||||||||||||||
Accepted name: | ABC-type polyamine transporter | ||||||||||||||||||
Reaction: | ATP + H2O + polyamine-[polyamine-binding protein][side 1] = ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1] | ||||||||||||||||||
Other name(s): | polyamine ABC transporter; polyamine-transporting ATPase | ||||||||||||||||||
Systematic name: | ATP phosphohydrolase (ABC-type, polyamine-importing) | ||||||||||||||||||
Comments: | An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially. | ||||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||||||
References: |
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