Wu3857 at 03:41, 28 April 2020

2020-04-28T03:41:47Z

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 P..."

2020-04-28T03:41:26Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 P..."

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{{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 Pyridoxal-dependent decarboxylase, C-terminal sheet domain],Orn/Lys/Arg decarboxylase class-II family|[[:Category:Ornithine decarboxylase|Ligand list]]|Metabolic enzyme}}

==Summary==

===Protein Function ===
Eukaryotic ornithine decarboxylase (ODC) is a pyridoxal 5’-phosphate (PLP)-dependent enzyme that catalyzes the initial step in the polyamine biosynthetic pathway, the decarboxylation of L-ornithine to produce putrescine. The polyamines putrescine, spermidine, and spermine are ubiquitous compounds that are essential for cell growth and differentiation in many organisms. 
They have demonstrated roles in cell cycle, apoptosis, cancer, embryonic development, immune system functions, and neurochemistry. Overexpression of polyamine biosynthetic enzymes leads to mammalian cell transformation or to growth perturbations in plants, whereas knockout of the polyamine biosynthetic enzymes causes polyamine auxotrophy (e.g. yeast, Trypanosoma brucei, and Leishmania donovani) and is lethal at early embryonic stages in mice. Inhibitors of polyamine biosynthetic enzymes have anti-proliferative effects and have been utilized as anticancer and anti-parasite agents. (PMID: 15190062) 

===Cys Function & Property===
Cys360 is the active site of Odc1 as a proton donor. 

* Hydrophobic property:
:[[File:599-hydro.png||600px]]
* SASA：
:Cys360: 121.3 A^2 

==Protein Sequence==

MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK 
KHLRWLKALP RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG 
LGVPAERVIY ANPCKQVSQI KYAASNGVQM MTFDSEIELM KVARAHPKAK 
LVLRIATDDS KAVCRLSVKF GATLKTSRLL LERAKELNID VIGVSFHVGS 
GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG SEDTKLKFEE 
ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ 
PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY 
YSSSIWGPT'''C''' DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF 
QRPNIYYVMS RPMWQLMKQI QSHGFPPEVE EQDDGTLPMS CAQESGMDRH 
PAACASARIN V 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
:[[File:599.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00330 Arginine and proline metabolism] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko00480 Glutathione metabolism] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko01100 Metabolic pathways] 

==Experimental Evidence==
:Mass Spectrometry, Homologous Analysis of Sequence

==Reference==
# Shah R, Coleman C S, Mir K, et al. Paramecium bursaria chlorella virus-1 encodes an unusual arginine decarboxylase that is a close homolog of eukaryotic ornithine decarboxylases[J]. Journal of Biological Chemistry, 2004, 279(34): 35760-35767. [https://www.ncbi.nlm.nih.gov/pubmed/?term=15190062 15190062] 
# Poulin R, Lu L, Ackermann B, et al. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites[J]. Journal of Biological Chemistry, 1992, 267(1): 150-158. [https://www.ncbi.nlm.nih.gov/pubmed/?term=1730582 1730582] 

[[Category:Targets]]
[[Category:Mus musculus]]
[[Category:Metabolic enzyme]]
[[Category:Pyridoxal-dependent decarboxylase, C-terminal sheet domain]]
[[Category:Metabolic pathways]]
[[Category:Arginine and proline metabolism]]
[[Category:Metabolic pathways]]

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-{{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 Pyridoxal-dependent decarboxylase, C-terminal sheet domain],Orn/Lys/Arg decarboxylase class-II family|[[:Category:Ornithine decarboxylase|Ligand list]]|Metabolic enzyme}}
+{{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 Pyridoxal-dependent decarboxylase, C-terminal sheet domain],<br/>Orn/Lys/Arg decarboxylase class-II family|[[:Category:Ornithine decarboxylase|Ligand list]]|Metabolic enzyme}}
 ==Summary==

Ornithine decarboxylase - Revision history

Wu3857 at 03:41, 28 April 2020

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 P..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|Odc1|[https://www.uniprot.org/uniprot/P00860 P00860]|Mus musculus|Cys360|[http://pfam.xfam.org/family/PF00278 P..."