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Literature summary for 1.5.1.30 extracted from

  • Duff, M.R.; Redzic, J.S.; Ryan, L.P.; Paukovich, N.; Zhao, R.; Nix, J.C.; Pitts, T.M.; Agarwal, P.; Eisenmesser, E.Z.
    Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family (2020), J. Biochem., 168, 191-202 .
    View publication on PubMed
Search for more literature for 1.5.1.30

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Homo sapiens
-
 Microcebus murinus

Protein Variants

Protein Variants Comment Organism
Q14R mutation at active site arginine residue increases coenzyme affinity Homo sapiens
Q14R/R78G double mutation within the enzyme exhibits a binding affinity that is close to the average between these two individual mutations Homo sapiens
R78R mutation at active site arginine residue weakens affinity slightly Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.236
-
 FAD pH and temperature not specified in the publication Microcebus murinus

Organism

Organism UniProt Comment Textmining
Homo sapiens P30043
-
-
Microcebus murinus XP_020138941.1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens
-
 Microcebus murinus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADPH + H+
-
 Homo sapiens FADH2 + NADP+
-
 ?
FAD + NADPH + H+
-
 Microcebus murinus FADH2 + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
biliverdin reductase B
-
 Homo sapiens
biliverdin reductase B
-
 Microcebus murinus
BLVRB
-
 Homo sapiens
BLVRB
-
 Microcebus murinus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information coenzyme clamps formed by arginine side chains at two co-evolving positions within the active site serve to slow coenzyme release (Positions 14 and 78). Coenzyme release is further slowed by the weaker binding substrate, resulting in relatively slow turnover numbers Homo sapiens
additional information
-
 additional information coenzyme clamps formed by arginine side chains at two co-evolving positions within the active site serve to slow coenzyme release (Positions 14 and 78). Coenzyme release is further slowed by the weaker binding substrate, resulting in relatively slow turnover numbers Microcebus murinus
0.061
-
 FAD pH and temperature not specified in the publication Microcebus murinus

General Information

General Information Comment Organism
evolution the study elucidates the role of the evolutionarily changing biliverdin reductase (BBLVRB) active site that serves to modulate coenzyme release and shows that coenzyme release is coupled to substrate turnover Homo sapiens
evolution the study elucidates the role of the evolutionarily changing biliverdin reductase (BBLVRB) active site that serves to modulate coenzyme release and shows that coenzyme release is coupled to substrate turnover Microcebus murinus