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Literature summary for 1.14.11.16 extracted from

  • Greve, J.M.; Pinkham, A.M.; Thompson, Z.; Cowan, J.A.
    Active site characterization and activity of the human aspartyl (asparaginyl) beta-hydroxylase (2021), Metallomics, 13, mfab056 .
    View publication on PubMed
Search for more literature for 1.14.11.16

Protein Variants

Protein Variants Comment Organism
D721A activity is 20% compared to wild-type activity Homo sapiens
E617A activity is 100% compared to wild-type activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.086
-
 [factor X first EGF-like domain]-L-aspartate pH and temperature not specified in the publication Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme binds divalent calcium, high-affinity regulatory binding site for Ca2+ Homo sapiens
Fe2+ nonheme Fe2+-dependent enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q12797
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[factor X first EGF-like domain]-L-aspartate + 2-oxoglutarate + O2
-
 Homo sapiens [factor X first EGF-like domain]-3-hydroxy-L-aspartate + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
aspartyl/asparaginyl beta-hydroxylase
-
 Homo sapiens
HAAH
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.23
-
 [factor X first EGF-like domain]-L-aspartate pH and temperature not specified in the publication Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
15
-
 [factor X first EGF-like domain]-L-aspartate pH and temperature not specified in the publication Homo sapiens