EC Number   |
General Information |
Reference  |
|---|
    1.3.98.3 | physiological function |
viperin is an interferon-inducible protein inhibiting a diverse spectrum of DNA and RNA viruses. It contains an N-terminal transmembrane helix, a highly conserved C-terminus and a middle region carrying a CX3CX2C motif, characteristic of radical S-adenosyl-L-methionine enzymes. The radical SAM enzyme activity may play a key role in the broad antiviral actions of viperin |
711084 |
| 1.3.98.3 | evolution |
in eukaryotes and some bacteria, oxidative decarboxylation of coproporphyrinogen III is performed by the oxygen-dependent CPO HemF, EC 1.3.3.3. In most bacteria, the reaction is catalyzed by the oxygen-independent enzyme HemN. HemN belongs to the family of radical S-adenosyl-L-methionine enzymes. HemF and HemN are structurally completely unrelated and show different catalytic mechanisms, overview |
711348 |
| 1.3.98.3 | more |
the interferon-inducible antiviral protein viperin is a radical SAM enzyme, immune response pathway involving viperin that leads to the disruption of viral release from the plasma membrane, overview |
712016 |
| 1.3.98.3 | physiological function |
catalyzes the decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX in heme biosynthesis and is shared in chlorophyll biosynthesis in photosynthetic organisms |
713258 |
| 1.3.98.3 | evolution |
HemW-like proteins form a distinct phylogenetic clade. It contains the four cysteine residues of the radical S-adenosyl-L-methionine enzyme motif of CPDH enzymes, structure comparisons, overview. The fourth cysteine residue of the Fe-S cluster motif of Escherichia coli HemN, CX3CX2CXC, is replaced by phenylalanine in HemW and related proteins |
724235 |
| 1.3.98.3 | metabolism |
genes hemH and hemW (hemN) show conjectured functions in heme metabolism |
724235 |
| 1.3.98.3 | physiological function |
addition of Lactococcus lactis membranes to heme-containing HemW triggers the release of heme from HemW in vitro. Role of HemW in heme trafficking |
724235 |
| 1.3.98.3 | evolution |
the anaerobic [4Fe-4S] containing enzymes have been replaced in metabolic pathways by more efficient and stable aerobic versions as a response and adaptation to oxygen appearance on earth, with copper damages [4Fe-4S] cluster under anaerobiosis or limited oxygen tensionplaying a role in the selection pressure leading to the evolution of copper/oxygen tolerant enzymes, copper targets the 4Fe-4S clusters in the anaerobic enzymes |
726009 |
| 1.3.98.3 | malfunction |
oxidized coproporphyrinogen III accumulates in a hemN2- mutant in Rubrivirax gelatinosus only under oxygen limited conditions |
726009 |
| 1.3.98.3 | metabolism |
the enzyme is involved in the O2-independent tetrapyrrole biosynthesis pathway, regulation overview |
726009 |
