2.5.1.44: homospermidine synthase
This is an abbreviated version!
For detailed information about homospermidine synthase, go to the full flat file.
Word Map on EC 2.5.1.44
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2.5.1.44
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knee
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arthroplasty
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postoperative
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pain
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tibial
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osteoarthritis
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acquity
-
preoperative
-
fracture
-
acetonitrile
-
radiograph
-
formic
-
medial
-
femoral
-
radiological
-
osteotomy
-
loosening
-
flexion
-
varus
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ultra-performance
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satisfaction
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inter-day
-
humic
-
womac
-
cement
-
radiolucent
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cruciate
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patella
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mcmaster
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arthroscopic
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unicompartmental
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uhplc
-
prostheses
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lysholm
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hepatosplenic
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leadership
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tegner
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heterostructures
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cementless
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deoxyhypusine
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malalignment
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kellgren-lawrence
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resurface
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condylar
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nonunion
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precisions
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posterolateral
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meniscal
-
curricula
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patellofemoral
- 2.5.1.44
- knee
-
arthroplasty
-
postoperative
- pain
- tibial
- osteoarthritis
-
acquity
-
preoperative
-
fracture
- acetonitrile
-
radiograph
-
formic
-
medial
-
femoral
-
radiological
-
osteotomy
-
loosening
-
flexion
- varus
-
ultra-performance
-
satisfaction
-
inter-day
-
humic
-
womac
-
cement
-
radiolucent
-
cruciate
-
patella
-
mcmaster
-
arthroscopic
-
unicompartmental
-
uhplc
-
prostheses
-
lysholm
-
hepatosplenic
-
leadership
-
tegner
-
heterostructures
-
cementless
- deoxyhypusine
-
malalignment
-
kellgren-lawrence
-
resurface
-
condylar
-
nonunion
-
precisions
-
posterolateral
-
meniscal
-
curricula
-
patellofemoral
Reaction
2 putrescine
=
Synonyms
Atu3768, BvHSS, homospermidine synthase orthologue, HSPD synthase, HSS, HSS orthologue, synthase, homospermidine
ECTree
2.5.1.44 homospermidine synthaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.5.1.44 - homospermidine synthase
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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
-
-
-
?
spermidine + cadaverine
(4-aminobutyl)(5-aminopentyl)amine + sym-homospermidine + propane-1,3-diamine + putrescine
-
-
-
?
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine
-
-
-
-
?
spermidine + putrescine
sym-homospermidine + propane-1,3-diamine + putrescine
-
-
-
?
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
-
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
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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
-
-
-
?
putrescine + 1,3-diaminopropane
homospermidine + spermidine
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-
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
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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
?
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
-
-
-
?
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
-
-
-
?
spermidine + cadaverine
homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
-
-
-
?
spermidine + putrescine
homospermidine + 1,3-diaminopropane
-
-
-
?
spermidine + putrescine
homospermidine + 1,3-diaminopropane
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
