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Information on EC 2.5.1.16 - spermidine synthase and Organism(s) Helicobacter pylori and UniProt Accession O25503

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EC Tree
IUBMB 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).
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This record set is specific for:
Helicobacter pylori
UNIPROT: O25503
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The taxonomic range for the selected organisms is: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
Synonyms
spermidine synthase, aminopropyltransferase, spds2, spdsyn, spd synthase, mdspds1, spermidine synthase 1, putrescine aminopropyltransferase, pgspd, spermidine synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyltransferase
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aminopropyltransferase spermidine synthase
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-
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putrescine aminopropyltransferase
spermidine synthetase
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synthase, spermidine
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
the enzyme possesses a Rossmann-like fold with a distinct active site, the enzyme from Helicobacter pylori lacks the gatekeeping loop that facilitates substrate binding in other PAPTs, active site structure
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminopropyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase
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).
CAS REGISTRY NUMBER
COMMENTARY hide
37277-82-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
show the reaction diagram
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-
-
ir
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
show the reaction diagram
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PAPTs are essential for bacterial cell viability
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of SpeE does not affect flagellar formation, but induces clockwise rotation bias
physiological function
the enzyme is required for normal motor function. It interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31900
calculated
123000
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tetrameric enzyme form B, analytical ultracentrifugation
158000
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tetrameric enzyme form B, gel filtration
30590
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calculated
58000
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dimeric enzyme form A, analytical ultracentrifugation
60000
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dimeric enzyme form A, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
tetramer
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dimer of dimer assembly, enzyme form B crystals, overview, the enzyme shows an N-terminal beta-stranded domain and a C-terminal Rossmann-like domain, structure comparison
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion at 16°C. Crystal structure of the FliMSpeE complex is determined at 2.7 A resolution
purified recombinant His6-tagged enzyme, also as selenomethionine-labeled enzyme, the latter from 0.1 M sodium HEPES, pH 7.5, with 33% PEG 400, two crystals Forms A and B, belonging to the monoclinic space group P21and orthorhombic space group C2221, are grown under different conditions, X-ray diffraction structure determination and analysis at 2.0-2.5 A resolution, multiwavelength anomalous dispersion
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain SG13009 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
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gene speE, sequence comparison, overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain SG13009 and in strain B834 for the selenomethionine-labeled enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, P.K.; Chien, S.Y.; Tsai, J.Y.; Fong, C.T.; Lee, M.J.; Huang, H.; Sun, Y.J.
Crystallization and preliminary X-ray diffraction analysis of spermidine synthase from Helicobacter pylori
Acta Crystallogr. Sect. D
60
2067-2069
2004
Helicobacter pylori
Manually annotated by BRENDA team
Lee, M.J.; Huang, C.Y.; Sun, Y.J.; Huang, H.
Cloning and characterization of spermidine synthase and its implication in polyamine biosynthesis in Helicobacter pylori strain 26695
Protein Expr. Purif.
43
140-148
2005
Helicobacter pylori (O25503), Helicobacter pylori
Manually annotated by BRENDA team
Lu, P.K.; Tsai, J.Y.; Chien, H.Y.; Huang, H.; Chu, C.H.; Sun, Y.J.
Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-like fold with a distinct active site
Proteins
67
743-754
2007
Helicobacter pylori
Manually annotated by BRENDA team
Zhang, H.; Lam, K.H.; Lam, W.W.L.; Wong, S.Y.Y.; Chan, V.S.F.; Au, S.W.N.
A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori
Mol. Microbiol.
106
690-703
2017
Helicobacter pylori (O25503), Helicobacter pylori
Manually annotated by BRENDA team