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Literature summary for 1.5.1.30 extracted from

  • Paukovich, N.; Xue, M.; Elder, J.R.; Redzic, J.S.; Blue, A.; Pike, H.; Miller, B.G.; Pitts, T.M.; Pollock, D.D.; Hansen, K.; DAlessandro, A.; Eisenmesser, E.Z.
    Biliverdin reductase B dynamics are coupled to coenzyme binding (2018), J. Mol. Biol., 430, 3234-3250 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.30

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
R78A mutation leads to both an increase in active site micro-millisecond motions and an increase in the microscopic rate constants of coenzyme binding Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P30043
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FAD + NADPH + H+ the enzyme (BLVRB) binds its coenzyme NADPH 500fold more tightly than its substrate FAD Homo sapiens FADH2 + NADP+
-
 ?

Synonyms

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

General Information

General Information Comment Organism
evolution most BLVRB enzymes have an arginine at either residue 14 or residue 78 (human numbering), although a subset maintain an arginine at both sites. In primates, the two substitutions are made on the same branch separating the common ancestor of the Simiiformes (apes, new and old-world monkeys) with the common ancestor of the Haplorhini (i.e., after the split from the common ancestor with the tarsier). This suggests possible adaptive coevolution at these two sites and adjusting the location of this arginine may serve to fine-tune coenzyme binding in BLVRB enzymes Homo sapiens