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Literature summary for 1.1.1.153 extracted from

  • Lange, I.; Geerts, D.; Feith, D.J.; Mocz, G.; Koster, J.; Bachmann, A.S.
    Novel interaction of ornithine decarboxylase with sepiapterin reductase regulates neuroblastoma cell proliferation (2014), J. Mol. Biol., 426, 332-346.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine siRNA-mediated knock-down of sepiapterin reductase expression significantly reduces endogenous ornithine decarboxylase enzyme activity in neuroblastoma cells. In a cohort of 88 human neuroblastoma tumors, high SPR mRNA expression correlates significantly with poor survival prognosis Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
silico protein-protein docking simulations to define the individual amino acid residues involved in the interaction between native ornithine decarboxylase and sepiapterin reductase Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information siRNA-mediated knockdown of SPR expression, significantly reduces endogenous ornithine decarboxylase enzyme activity in neuroblastoma cells and leads to a significant and consistent decrease in cellular proliferation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens native ornithine decarboxylase, EC 4.1.1.17, and sepiapterin reductase physically interact, in silico protein-protein docking simulations ?
-
?
sepiapterin + NADPH + H+ Homo sapiens
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tetrahydrobiopterin + NADP+ no stereochemic specification in the publication ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P35270
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293 cell
-
Homo sapiens
-
MYCN2 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information native ornithine decarboxylase, EC 4.1.1.17, and sepiapterin reductase physically interact, in silico protein-protein docking simulations Homo sapiens ?
-
?
sepiapterin + NADPH + H+
-
Homo sapiens tetrahydrobiopterin + NADP+ no stereochemic specification in the publication ?

Subunits

Subunits Comment Organism
homodimer
-
Homo sapiens
More in silico protein-protein docking simulationsof enzyme SPR with ornithine decraboxylase, ODC, structure analysis, overview Homo sapiens

Synonyms

Synonyms Comment Organism
sepiapterin reductase
-
Homo sapiens
SPR
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Homo sapiens

General Information

General Information Comment Organism
malfunction the knockdown of SPR leads to a significant and consistent decrease in cellular proliferation of neuroblastoma cells Homo sapiens
physiological function native ornithine decarboxylase and sepiapterin reductase physically interact. The resulting heterocomplex is a compact structure, featuring two energetically and structurally equivalent binding modes both in monomer and dimer conformations. siRNA-mediated knock-down of sepiapterin reductase expression significantly reduces endogenous ornithine decarboxylase enzyme activity in neuroblastoma cells Homo sapiens
physiological function sepiapterin reductase (SPR) catalyzes the last step in the biosynthesis of tetrahydrobiopterin (BH4) by converting 6-pyruvoyl tetrahydropterin to tetrahydrobiopterin. BH4 is an essential cofactor of nitric oxide synthase (NOS), which converts arginine to nitric oxide (NO) and citrulline in the urea cycle. Native ornithine decarboxylase, ODC, EC 4.1.1.17, and sepiapterin reductase physically interact, SPR is a regulator of ODC activity. SPR is implicated in neurological diseases and in cancer. SPR contributes to neuroblastoma cell proliferation and regulates ODC enzyme activity in neuroblastoma cells, ODC-SPR interaction controls polyamine-driven cellular proliferation Homo sapiens