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Your query returned 22 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 | ||||||||||||||||
References: |
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EC | 1.5.3.3 | ||||||||||||||||
Deleted entry: | spermine oxidase | ||||||||||||||||
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 | ||||||||||||||||
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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 = 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 | 2.3.1.57 | ||||||||||||||||
Accepted name: | diamine N-acetyltransferase | ||||||||||||||||
Reaction: | acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine | ||||||||||||||||
Glossary: | spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine.html">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 | 2.5.1.16 | ||||||||||||||||
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 = N-(3-aminopropyl)butane-1,4-diamine spermine.html">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 = N-(3-aminopropyl)butane-1,4-diamine spermine.html">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 | ||||||||||||||||
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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 | 2.5.1.126 | ||||||||||||||||
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 | 3.5.1.48 | ||||||||||||||||
Accepted name: | acetylspermidine deacetylase | ||||||||||||||||
Reaction: | N8-acetylspermidine + H2O = acetate + spermidine | ||||||||||||||||
Glossary: | spermidine = N-(3-aminopropyl)butane-1,4-diamine spermine.html">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 | 4.1.1.17 | ||||||||||||||||
Accepted name: | ornithine decarboxylase | ||||||||||||||||
Reaction: | L-ornithine = putrescine + CO2 | ||||||||||||||||
For diagram of spermine biosynthesis, click here and for diagram of arginine catabolism, click here | |||||||||||||||||
Glossary: | putrescine = butane-1,4-diamine | ||||||||||||||||
Other name(s): | SpeC; L-ornithine carboxy-lyase | ||||||||||||||||
Systematic name: | L-ornithine carboxy-lyase (putrescine-forming) | ||||||||||||||||
Comments: | A pyridoxal-phosphate protein. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-60-6 | ||||||||||||||||
References: |
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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 | 4.1.1.116 | ||||||||||||||||
Accepted name: | D-ornithine/D-lysine decarboxylase | ||||||||||||||||
Reaction: | (1) D-ornithine = putrescine + CO2 (2) D-lysine = cadaverine + CO2 |
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For diagram of spermine biosynthesis, click here | |||||||||||||||||
Glossary: | cadaverine = pentane-1,5-diamine putrescine = butane-1,4-diamine |
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Other name(s): | dokD (gene name); DOKDC | ||||||||||||||||
Systematic name: | D-ornithine/D-lysine carboxy-lyase | ||||||||||||||||
Comments: | The enzyme, characterized from the bacterium Salmonella typhimurium LT2, is specific for D-ornithine and D-lysine. Requires pyridoxal 5′-phosphate. | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||||
References: |
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EC | 5.1.1.12 | ||||||||||||||||
Accepted name: | ornithine racemase | ||||||||||||||||
Reaction: | L-ornithine = D-ornithine | ||||||||||||||||
For diagram of spermine biosynthesis, click here | |||||||||||||||||
Systematic name: | ornithine racemase | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-28-9 | ||||||||||||||||
References: |
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