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Q44777437-ABDA41CA-4E8B-4DCB-9F30-0C064D0F0809
Q44777437-ABDA41CA-4E8B-4DCB-9F30-0C064D0F0809
BestRank
Statement
http://www.wikidata.org/entity/statement/Q44777437-ABDA41CA-4E8B-4DCB-9F30-0C064D0F0809
Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half.
P2860
Q44777437-ABDA41CA-4E8B-4DCB-9F30-0C064D0F0809
BestRank
Statement
http://www.wikidata.org/entity/statement/Q44777437-ABDA41CA-4E8B-4DCB-9F30-0C064D0F0809
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wasDerivedFrom
2db76268231623daa679a31405e03af6fd0ae9ef
P2860
Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides.