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Enzyme Nomenclature
Information on EC 2.5.1.44 - homospermidine synthase
Word Map on EC 2.5.1.44
- 2.5.1.44
-
pyrrolizidine
- deoxyhypusine
-
alkaloid
-
polyamine
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asteraceae
-
angiosperm
- senecio
- vernalis
-
herbivores
-
pathway-specific
-
pa-producing
- triamine
-
rhodopseudomonas
- agmatine
-
aminobutylation
- viridis
- 1,7-diaminoheptane
- 1,3-diaminopropane
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heliotropium
-
kaiser
- cadaverine
- officinale
- indicum
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.5.1.44
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RECOMMENDED NAME
GeneOntology No.
homospermidine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 putrescine = sym-homospermidine + NH3 + H+
the reaction of this enzyme occurs in three steps: i. NAD-dependent dehydrogenation of putrescine, ii. transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine, iii. reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. In the presence of putrescine, spermidine can function as a donor of the aminobutyl group, in which case, propane-1,3-diamine is released instead of ammonia. Differs from EC 2.5.1.45, homospermidine synthase, spermidine-specific, which cannot use putrescine as donor of the aminobutyl group
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-
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2 putrescine = sym-homospermidine + NH3 + H+
the reaction mechanism emphasizes cation-Pi interaction through a conserved Trp residue as a key stabilizer of high energetic transition states. The enzyme has two distinct substrate binding sites, one of which is highly specific for putrescine. Enzyme HSS features a side pocket in the direct vicinity of the active site formed by conserved amino acids and a potential substrate discrimination, guiding, and sensing mechanism
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
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-
-
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putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
the reaction mechanism emphasizes cation-Pi interaction through a conserved Trp residue as a key stabilizer of high energetic transition states. The enzyme has two distinct substrate binding sites, one of which is highly specific for putrescine. Enzyme HSS features a side pocket in the direct vicinity of the active site formed by conserved amino acids and a potential substrate discrimination, guiding, and sensing mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminobutyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)
The reaction of this enzyme occurs in three steps, with some of the intermediates presumably remaining enzyme-bound: NAD+-dependent dehydrogenation of putrescine, transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine and reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.
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CAS REGISTRY NUMBER
COMMENTARY
76106-84-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acinetobacter tartarogenes
accession no. L77975; DSM 134; expressed in Escherichia coli strain BL21/pHsRvT72.2
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
in Paramecium, a bacterial homospermidine synthase replaces the eukaryotic genes encoding spermidine biosynthesis, S-adenosylmethionine decarboxylase and spermidine synthase. The Paramecium tetraurelia macronuclear genome does not encode any homologues of S-adenosylmethionine decarboxylase and spermidine synthase. Many eukaryotic parasites have lost the entire spermidine biosynthetic pathway but have in all cases retained the deoxyhypusine synthase gene required to post-translationally modify eIF5A. Replacement of spermidine with homospermidine is compatible with hypusine modification of eIF5A, loss of dependence on S-adenosylmethionine decarboxylase for spermidine biosynthesis has the benefit ofdispensing with the use of metabolically expensive S-adenosyl-L-methionine and the methionine salvage pathway required to rescue methionine from methylthioadenosine, the coproduct of spermidine synthase
evolution
bacterial homospermidine synthase is highly conserved and is proposed to be evolutionarily related to carboxy(nor)spermidine dehydrogenase, EC 1.5.1.43. Despite of the low amino acid sequence identity between plant HSS and bacterial HSS of about 12% (Senecio vulgaris vs. Blastochloris viridis HSS), a conserved fold within the three dimensional structure of bacterial HSS might be responsible for the similarity of the reaction mechanism
evolution
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in Paramecium, a bacterial homospermidine synthase replaces the eukaryotic genes encoding spermidine biosynthesis, S-adenosylmethionine decarboxylase and spermidine synthase. The Paramecium tetraurelia macronuclear genome does not encode any homologues of S-adenosylmethionine decarboxylase and spermidine synthase. Many eukaryotic parasites have lost the entire spermidine biosynthetic pathway but have in all cases retained the deoxyhypusine synthase gene required to post-translationally modify eIF5A. Replacement of spermidine with homospermidine is compatible with hypusine modification of eIF5A, loss of dependence on S-adenosylmethionine decarboxylase for spermidine biosynthesis has the benefit ofdispensing with the use of metabolically expensive S-adenosyl-L-methionine and the methionine salvage pathway required to rescue methionine from methylthioadenosine, the coproduct of spermidine synthase
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malfunction
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sym-homospermidine is required for normal growth of the alpha-proteobacterium Rhizobium leguminosarum. Symhomospermidine can be replaced, for growth restoration, by the structural analogues spermidine and symnorspermidine, suggesting that the symmetrical or unsymmetrical form, and carbon backbone length are not critical for polyamine function in growth
malfunction
ann enzyme knockout mutant does not contain neither homospermidine nor 4-aminobutilcadaverine and is more sensitive to salinity than the wild-type, and plants inoculated with the mutant bacteria have lower nodule fresh weight than with the wild-type
malfunction
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ann enzyme knockout mutant does not contain neither homospermidine nor 4-aminobutilcadaverine and is more sensitive to salinity than the wild-type, and plants inoculated with the mutant bacteria have lower nodule fresh weight than with the wild-type
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metabolism
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Paramecium tetraurelia performs spermidine biosynthesis by aminopropylation of putrescine with production of methylthioadenosine from decarboxylated S-adenosylmethionine, it accumulates homospermidine and shows absence of a methionine salvage pathway. Paramecium tetraurelia encodes four paralogues of bacterial homospermidine synthase, and at least one of those paralogues is enzymatically active in vitro. Paramecium accumulates homospermidine, suggesting it replaces spermidine for growth. Paramecium tetraurelia encodes four paralogues of bacterial homospermidine synthase, and at least one of those paralogues is enzymatically active in vitro. Homospermidine supports eukaryotic cell growth and proliferation
metabolism
essential enzyme of the bacterial polyamine metabolism
metabolism
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Paramecium tetraurelia performs spermidine biosynthesis by aminopropylation of putrescine with production of methylthioadenosine from decarboxylated S-adenosylmethionine, it accumulates homospermidine and shows absence of a methionine salvage pathway. Paramecium tetraurelia encodes four paralogues of bacterial homospermidine synthase, and at least one of those paralogues is enzymatically active in vitro. Paramecium accumulates homospermidine, suggesting it replaces spermidine for growth. Paramecium tetraurelia encodes four paralogues of bacterial homospermidine synthase, and at least one of those paralogues is enzymatically active in vitro. Homospermidine supports eukaryotic cell growth and proliferation
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physiological function
homospermidine synthase contributes to salt tolerance in free-living Rhizobium tropici and in symbiosis with Phaseolus vulgaris. Homospermidine is involved in the stress tolerance of fast-growing rhizobia and in the bacteroid protection from environmental changes. The enzyme seems to be involved in nodule organogenesis, the enzyme HSS is not required for normal growth of Rhizobium tropici but provides tolerance to salt stress, growth kinetics in wild-type and mutant strains, overview
physiological function
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homospermidine synthase contributes to salt tolerance in free-living Rhizobium tropici and in symbiosis with Phaseolus vulgaris. Homospermidine is involved in the stress tolerance of fast-growing rhizobia and in the bacteroid protection from environmental changes. The enzyme seems to be involved in nodule organogenesis, the enzyme HSS is not required for normal growth of Rhizobium tropici but provides tolerance to salt stress, growth kinetics in wild-type and mutant strains, overview
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additional information
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homospermidine is a structural analogue of spermidine that is one methylene group longer, rendering homospermidine symmetrical
additional information
the structure of the bacterial enzyme does not possess a lysine residue in the active center and does not form an enzyme-substrate Schiff base intermediate as observed for deoxyhypusine synthase. The active site is not formed by the interface of two subunits but resides within one subunit of the bacterial enzyme. The enzyme has two distinct substrate binding sites, one of which is highly specific for putrescine. Enzyme HSS features a side pocket in the direct vicinity of the active site formed by conserved amino acids and a potential substrate discrimination, guiding, and sensing mechanism. Three-dimensional structure analysis, PDB ID 4PLP, and substrate binding analysis
additional information
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homospermidine is a structural analogue of spermidine that is one methylene group longer, rendering homospermidine symmetrical
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 spermidine
sym-homospermidine + propane-1,3-diamine + putrescine
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-
-
?
spermidine + cadaverine
(4-aminobutyl)(5-aminopentyl)amine + sym-homospermidine + propane-1,3-diamine + putrescine
-
-
-
?
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine + putrescine
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
-
?
2 putrescine
sym-homospermidine + NH3
-
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
-
?
2 putrescine
sym-homospermidine + NH3
-
as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45
-
?
2 putrescine
sym-homospermidine + NH3
-
as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45
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?
putrescine + 1,3-diaminopropane
homospermidine + spermidine
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-
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putrescine + 1,3-diaminopropane
homospermidine + spermidine
-
-
low but significant amounts of homologous polyamines in addition to homospermidine
?
putrescine + 1,6 diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
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-
-
?
putrescine + 1,6 diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
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-
low but significant amounts of homologous polyamines in addition to homospermidine
?
putrescine + 1,7-diaminoheptane
homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
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-
-
-
putrescine + 1,7-diaminoheptane
homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
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low but significant amounts of homologous polyamines in addition to homospermidine
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putrescine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
-
-
-
?
putrescine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
-
-
low but significant amounts of homologous polyamines in addition to homospermidine
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
-
-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
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-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
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-
-
?
spermidine
homospermidine + putrescine + 1,3-diaminopropane
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-
-
?
spermidine
homospermidine + putrescine + 1,3-diaminopropane
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-
-
?
spermidine + 1,6-diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
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-
-
?
spermidine + 1,6-diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
-
-
-
?
spermidine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
-
-
-
?
spermidine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
-
-
-
?
spermidine + putrescine
homospermidine + 1,3-diaminopropane
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-
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?
spermidine + putrescine
homospermidine + 1,3-diaminopropane
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-
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?
additional information
?
-
the enzyme has two distinct substrate binding sites, one of which is highly specific for putrescine. Enzyme HSS features a side pocket in the direct vicinity of the active site formed by conserved amino acids and a potential substrate discrimination, guiding, and sensing mechanism. The enzyme is capable of catalyzing side reactions to produce a variety of N-aminobutyl-linked triamines utilizing putrescine together with respective linear diamines with C3 to C7 carbon chains, overview. Bacterial HSS does not produce sym-norspermidine from two 1,4-diaminopropanes
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additional information
?
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despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
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-
-
additional information
?
-
despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 putrescine
sym-homospermidine + NH3
-
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
-
?
2 putrescine
sym-homospermidine + NH3
-
one molecule of putrescine is oxidized by NAD+ to form enzyme-bound 4-aminobutyraldehyde. This intermediate reacts with a second molecule of putrescine to form a Schiff base which is reduced by NADH (formed from NAD+ in the first part of the reaction) to give homospermidine
-
?
2 putrescine
sym-homospermidine + NH3
-
as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45
-
?
2 putrescine
sym-homospermidine + NH3
-
as partially purified enzymes have been used in the assay the dependence on spermidine for the homospermidine synthesis may have been overlooked. If these enzymes should proof to be spermidine-dependent like other enzymes from plant sources, they must be classified as EC 2.5.1.45
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
O32323
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-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
L0LQI4
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-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
L0LQI4
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-
-
?
additional information
?
-
L0LQI4
despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
-
-
-
additional information
?
-
L0LQI4
despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
unique usage of NAD(H) as a prosthetic group. the cofactor is coordinated through hydrogen bonding via residues Ser21, Ile22, Ser230 (phosphate), Asp45, Val66 (adenosine), Ser92,Thr114, Ala161, Asn162, and Pro163 (nicotineamide riboside). The phosphate-binding motif (18GFGSIG23) is located in the loop connecting beta-strand 2 and alpha-helix A of the Rossmann fold. The adenosine part of NAD+ is bound via loop regions located between beta-strand 4, 5, 6 and alpha-helix C, D, E. Nicotineamide-riboside-binding residues are found in loop regions between beta-strand 7 and 8 and alpha-helix F and O
NAD+
-
cannot be replaced by NADP+, NADPH, NADH; required in catalytic amounts with a Km-value of 0.0025 mM
NAD+
-
NAD+ seems to function as hydride acceptor in the first part of the reaction and subsequently as hydride donor in the second part
NAD+
unique usage of NAD(H) as a prosthetic group. the cofactor is coordinated through hydrogen bonding via residues Ser21, Ile22, Ser230 (phosphate), Asp45, Val66 (adenosine), Ser92,Thr114, Ala161, Asn162, and Pro163 (nicotineamide riboside). The phosphate-binding motif (18GFGSIG23) is located in the loop connecting beta-strand 2 and alpha-helix A of the Rossmann fold. The adenosine part of NAD+ is bound via loop regions located between beta-strand 4, 5, 6 and alpha-helix C, D, E. Nicotineamide-riboside-binding residues are found in loop regions between beta-strand 7 and 8 and alpha-helix F and O
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
Acinetobacter tartarogenes
-
preincubation, 1 mM, 30 min prior to assay causes 50% inhibition
additional information
-
4-aminobutyraldehyde, postulated intermediate, no inhibition
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N-ethylmaleimide
Acinetobacter tartarogenes
-
preincubation, 1 mM, 30 min prior to assay causes 91% inhibition
N-ethylmaleimide
-
inhibition suggests, that the enzyme is of a thiol nature
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
37
-
reaction linear up to 60 min and is proportional to the amount of enzyme protein (0.1-0.5 mg)
45
-
increasing activity up to 45°C, sharp decrease at higher temperatures
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
crude extract after ultrasonication and centrifugation
-
crude extract after ultrasonication and centrifugation
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 52000, SDS-PAGE; 2 * 52600, calculated from the amino acid sequence
dimer
the active site is not formed by the interface of two subunits but resides within one subunit of the bacterial enzyme, structure analysis
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the BvHSS structure is solved from crystals belonging to space group P212121 with bound NAD+, PDB ID 4PLP. Crystals from BvHSS and BvHSS variants with bound NAD+ in complex with various polyamines all belong to space group P22121 with cell parameters in approximately the same order of magnitude. Structure analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, storage as acetone dry-powder, without significant loss of activity
-
1°C, 20 mM, Tris/HCl, pH 7.5, 10 mM 2-mercaptoethanol, 0.5 mM putrescine, 0.02% NaN3
Acinetobacter tartarogenes
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
overexpressed in Escherichia coli BL21, which originally does not possess HSS activity. 40-50% of the soluble protein in crude extracts are detected as homospermidine synthase
-
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
Acinetobacter tartarogenes
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expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
-
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
-
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
expressed in Escherichia coli. The host Escherichia coli cells without the recombinant homospermidine synthase orthologue accumulate putrescine, cadaverine and spermidine and expression of each the homospermidine syntase orthologue in Escherichia coli results in accumulation of homospermidine in the host cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E237Q
site-directed mutagenesis, altered active site structure and impaired subsrate binding compared to wild-type, overview
H296S
site-directed mutagenesis, altered active site structure and impaired subsrate binding compared to wild-type, overview
additional information
additional information
construction of a mutant strain Rt hss::omega,Spr of Rhizobium tropici strain Rt CIAT899 impaired in the synthesis of homospermidine, neither homospermidine nor 4-aminobutilcadaverine are detected in the free-living mutant bacteria and in nodules of plants inoculated with the mutant strain
additional information
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construction of a mutant strain Rt hss::omega,Spr of Rhizobium tropici strain Rt CIAT899 impaired in the synthesis of homospermidine, neither homospermidine nor 4-aminobutilcadaverine are detected in the free-living mutant bacteria and in nodules of plants inoculated with the mutant strain
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