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
-
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
- 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 (Cofactor
Cofactor on EC 2.5.1.44 - homospermidine synthase
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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+
-
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
