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IUBMB CommentsThe 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.
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2 putrescine = sym-homospermidine + NH3 + H+
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
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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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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-
-
-
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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2 putrescine
sym-homospermidine + NH3
2 spermidine
sym-homospermidine + propane-1,3-diamine + putrescine
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-
-
?
putrescine
sym-homospermidine + NH3 + H+
putrescine + 1,3-diaminopropane
homospermidine + spermidine
putrescine + 1,6 diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
putrescine + 1,7-diaminoheptane
homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
putrescine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
spermidine
homospermidine + putrescine + 1,3-diaminopropane
spermidine + 1,6-diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
spermidine + cadaverine
(4-aminobutyl)(5-aminopentyl)amine + sym-homospermidine + propane-1,3-diamine + putrescine
-
-
-
?
spermidine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
spermidine + putrescine
homospermidine + 1,3-diaminopropane
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine
-
-
-
-
?
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine + putrescine
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-
-
?
additional information
?
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2 putrescine
sym-homospermidine + NH3
Acinetobacter tartarogenes
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-
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?
2 putrescine
sym-homospermidine + NH3
Acinetobacter tartarogenes
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-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
the enzyme is involved in polyamine biosynthesis pathway
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-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
the enzyme is involved in polyamine biosynthesis pathway
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?
2 putrescine
sym-homospermidine + NH3
-
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
-
?
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
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?
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
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?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
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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?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
-
?
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
sym-homospermidine + NH3 + H+
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-
-
?
putrescine
sym-homospermidine + NH3 + H+
-
-
-
?
putrescine
sym-homospermidine + NH3 + H+
-
-
-
?
putrescine + 1,3-diaminopropane
homospermidine + spermidine
-
-
-
?
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
-
-
-
?
putrescine + 1,6 diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
-
-
low but significant amounts of homologous polyamines in addition to homospermidine
?
putrescine + 1,7-diaminoheptane
homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
-
-
-
?
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
?
putrescine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
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-
-
?
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
-
-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
-
-
-
?
spermidine
homospermidine + putrescine + 1,3-diaminopropane
-
-
-
?
spermidine
homospermidine + putrescine + 1,3-diaminopropane
-
-
-
?
spermidine + 1,6-diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
-
-
-
?
spermidine + 1,6-diaminohexane
homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
-
-
-
?
spermidine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
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-
-
?
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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?
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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-
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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2 putrescine
sym-homospermidine + NH3
putrescine
sym-homospermidine + NH3 + H+
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine
-
-
-
-
?
additional information
?
-
2 putrescine
sym-homospermidine + NH3
Acinetobacter tartarogenes
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-
-
?
2 putrescine
sym-homospermidine + NH3
the enzyme is involved in polyamine biosynthesis pathway
-
-
?
2 putrescine
sym-homospermidine + NH3
the enzyme is involved in polyamine biosynthesis pathway
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
2 putrescine
sym-homospermidine + NH3
-
-
-
?
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
sym-homospermidine + NH3 + H+
-
-
-
?
putrescine
sym-homospermidine + NH3 + H+
-
-
-
?
putrescine
sym-homospermidine + NH3 + H+
-
-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
-
-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
-
-
-
?
putrescine + spermidine
sym-homospermidine + propane-1,3-diamine
-
-
-
?
additional information
?
-
despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
-
-
?
additional information
?
-
despite the synthesis of homospermidine, the enzyme also produces 4-aminobutilcadaverine
-
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?
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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
NADP+
-
68% of the activity with NAD+
NAD+
-
-
NAD+
Acinetobacter tartarogenes
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NAD+
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absolute requirement
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+
-
cannot be replaced by NADP+, NADPH, NADH
NAD+
-
required in catalytic amounts with a Km-value of 0.0025 mM
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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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
-
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
-
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
-
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
deletion of hss has no effect on polyamine levels in an otherwise wild-type strain, but in the CASDH mutant, it completely abolishes the increased Hspd levels. The DELTAhss mutant is also unaffected for prototrophic growth in the wild type, and this mutation does not alter the growth phenotypes of the DELTACASDH mutant
malfunction
-
deletion of hss has no effect on polyamine levels in an otherwise wild-type strain, but in the CASDH mutant, it completely abolishes the increased Hspd levels. The DELTAhss mutant is also unaffected for prototrophic growth in the wild type, and this mutation does not alter the growth phenotypes of the DELTACASDH mutant
-
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
-
metabolism
essential enzyme of the bacterial polyamine metabolism
metabolism
-
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
-
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
deletion of HSS has no effect on polyamine levels in an otherwise wild-type strain. In the CASDH mutant, lacking carboxyspermidine dehydrogenase activity, it completely abolishes the increased homospermidine levels. The HSS mutant is also unaffected for prototrophic growth in the wild type, and the mutation does not alter the growth phenotypes of the CASDH mutant
physiological function
-
the enzyme seems to be involved in nodule organogenesis and salt tolerance. Homospermidine synthase contributes to salt stress in both free-living and symbiotic bacteria
physiological function
-
deletion of HSS has no effect on polyamine levels in an otherwise wild-type strain. In the CASDH mutant, lacking carboxyspermidine dehydrogenase activity, it completely abolishes the increased homospermidine levels. The HSS mutant is also unaffected for prototrophic growth in the wild type, and the mutation does not alter the growth phenotypes of the CASDH mutant
-
physiological function
-
the enzyme seems to be involved in nodule organogenesis and salt tolerance. Homospermidine synthase contributes to salt stress in both free-living and symbiotic bacteria
-
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
-
additional information
-
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
-
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
-
homospermidine is a structural analogue of spermidine that is one methylene group longer, rendering homospermidine symmetrical
-
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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
expression as an untagged protein in Escherichia coli BL21
-
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
-
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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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
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Agrobacterium tumefaciens
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