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1.3.1.24: biliverdin reductase

This is an abbreviated version!
For detailed information about biliverdin reductase, go to the full flat file.

Word Map on EC 1.3.1.24

Reaction

bilirubin
+
NAD(P)+
=
Biliverdin
 +
NAD(P)H
 +
H+

Synonyms

biliverdin IXalpha reductase, biliverdin IXbeta reductase, biliverdin reductase, biliverdin reductase A, biliverdin reductase B, Biliverdin reductase-A, biliverdin-IXalpha reductase, BLVR subtype B, BLVRA, BLVRB, BV reductase, BVR, BVR-A, BVR-B, BVRA, BVRB, F-BVR, F420H2-dependent biliverdin reductase, hBVR, hBVR-A, reductase, biliverdin, Rv2074, slr1784

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.24 biliverdin reductase

Engineering

Engineering on EC 1.3.1.24 - biliverdin reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C281A/C292A/C293A
H132A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R124A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R172A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R172E
inactive
R172K
inactive
R174A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R18Stop
R35A
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R35S
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R39A
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
R78A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
S111A
the mutant shows strongly reduced activity compared to the wild type enzyme
S111L
the mutant shows strongly reduced activity compared to the wild type enzyme
V11A/V12A/V13A/V14A
-
not only fails to activate protein kinase C but also decreases its activity by 22%
W116A
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
W116F
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
Y198F
-
mutant, phosphorylation site
Y98F
the mutant shows about wild type catalytic efficiency
E47A
-
mutant, does affect the edge of the beta2 strand of substrate and cofactor binding in the pocket, which likely influences the strength of their interaction with BVR
E97A
-
mutant, data strongly support this site as important for conversion of biliverdin to bilirubin and for transmission of signaling by BVR
C280A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 280 principally functions in substrate binding
C291A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 291 is predominantly involved in cofactor binding.
C73A
-
the modification of the amino-proximal cysteine, which is flanked by a tyrosine residue, completely inactivates the enzyme with NADH at pH 6.75 and NADPH at pH 8.7
R171A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171E
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y98F
the mutant shows about wild type catalytic efficiency
K237A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R185A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R185K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R188A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R246A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S184A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T169A
the mutant shows wild type catalytic efficiency
Y102F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information