|
Your query returned 10 entries. Printable version
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+ |
||||||||||||||
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: |
| ||||||||||||||
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: |
| ||||||||||||||
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: |
| ||||||||||||||
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 = 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 |
||||||||||||||
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: |
| ||||||||||||||
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 = 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 |
||||||||||||||
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: |
| ||||||||||||||
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: |
| ||||||||||||||
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: |
| ||||||||||||||
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 |
||||||||||||||
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: |
| ||||||||||||||
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 |
||||||||||||||
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: |
| ||||||||||||||
EC | 4.1.1.96 | ||||||||||||||
Accepted name: | carboxynorspermidine decarboxylase | ||||||||||||||
Reaction: | (1) carboxynorspermidine = bis(3-aminopropyl)amine + CO2 (2) carboxyspermidine = spermidine + CO2 |
||||||||||||||
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: |
| ||||||||||||||