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1.6.2.2: cytochrome-b5 reductase

This is an abbreviated version!
For detailed information about cytochrome-b5 reductase, go to the full flat file.

Word Map on EC 1.6.2.2

Reaction

NADH
+ 2 ferricytochrome b5 =
NAD+
 +
H+
 + 2 ferrocytochrome b5

Synonyms

b5 plusb5R, b5/b5R, B5R, cb5r, CBR, CBR1, CBR1A, CBR1B, CyB5R, CYB5R2, CYB5R3, Cyb5R4, cyt b5r, cyt b5R protein, cytochrome b5 reductase, cytochrome b5 reductase 2, cytochrome b5 reductase 3, DIA1, diaphorase I, dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase, HPO-19, methemoglobin reductase, NADH cytochrome b5 oxidoreductase, NADH cytochrome B5 reductase, NADH-b5R, NADH-cytochrome b 5 reductase, NADH-cytochrome b5 reductase, NADH-cytochrome b5 reductase 3, NADH-cytochrome-b5 reductase, NADH-cytochrome-b5 reductase 3, NADH-dependent cytochrome b5 reductase, NADH-ferricyanide reductase, NADH-ferricytochrome b5 oxidoreductase, NADH-ferricytochrome reductase, NADH: ferricytochrome b5 oxidoreductase, NADH:cytochrome b5 reductase, NADH:ferricytochrome b5 oxidoreductase, Ncb5or, P34/P32, P35, reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase, reductase, cytochrome b5, T05H4.4

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.2 cytochrome-b5 reductase

Engineering

Engineering on EC 1.6.2.2 - cytochrome-b5 reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A178T
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 16.6% of wild-type enzyme activity
A179T
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
A179V
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
C204R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
C204Y
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
D239G
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant shows decreased specificity for NADH and increased specificity for NADPH, 28.5% of wild-type enzyme activity
D239T
-
the mutation changes the enzme preference for NADH to one for NADPH. Diseases related to CyB5R dysfunctions due to mutations in the gene encoding the enzyme, detailed overview
D240G
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
E213K
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
E255-
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type
F157C
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G143D
mutation in the NADH-cytochrome b5 reductase gene in an Indian patient with type I recessive hereditary methemoglobinemia
G144D
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G291D
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type and 35.2% of wild-type enzyme activity
G292D
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G72A
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
G75S
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
G75S/V252M
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
G76S
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
I216T
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
K110A
-
200fold elevated Km value for NADH, 85% of kcat
K110M
-
1120fold elevated Km value for NADH
K110R
-
similar kinetic properties as wild-type
K125A
-
5.3fold elevated Km value for cytochrome b5
K163A
-
5.7fold elevated Km value for cytochrome b5
K41A
-
6.3fold elevated Km value for cytochrome b5
L149P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L217P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L218P
-
the mutation is associated with type I recessive congenital methemoglobinemia
L239R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
L73P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
M127V
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P145L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P145S
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P275L
natural mutant from a patient with recessive congenital methemoglobinemia. Significant decrease in the affinity toward the physiological reducing substrate, NADH, without affecting the activity
P276L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P65L
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
P96H
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R159-/D239G
-
natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 40.8% of wild-type enzyme activity
R241G
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R259W
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R46W
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R50Q
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
R58Q
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
S128P
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
S54R
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
V106M
-
naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations
V172L
-
the mutation leads to recessive congenital methaemoglobinaemia type I
V252M
-
natural mutation isolated in patient with recessive congenital methemoglobinaemia. Mutant retains stoichiometric levels of FAD, but shows decreased catalytic efficiency and reduced protein stability
V253M
D239E
decreased activity with NADH and NADPH
D239S
significantly increased activity with NADPH
D239S/F251R
specific for NADPH
D239S/F251Y
bispecific for NADH and NADPH
D239T
specific for NADPH, 11fold preference for NADPH over NADH
D239T/F251R
specific for NADPH
F251R
minor effects on activity
F251Y
minor effects on activity
G179A
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179P
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179T
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
G179V
mutant preceeding the 180GxGxxP185 motif bindin the adenosine moiety of NAD(P)H. Incorporation of FAD and adsortion and CD spectra similar to wild-type. Decrease in NADH:ferricyanide activity and affinity for NADH
K110A
strongly reduced kcat for ferricyanide and cytochrome b5
K110E
strongly reduced kcat for ferricyanide and cytochrome b5
K110H
strongly reduced kcat for ferricyanide and cytochrome b5
K110Q
very low kcat for ferricyanide and cytochrome b5
K110R
reduced kcat for ferricyanid and cytochrome b5
L148P
31% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P144L
28% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P144L/L148P
8% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+
P92A
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
P92G
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
P92S
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
R159
deletion mutant, could not be successfully expressed
S127P
-
caused methemoglobinemia type II, FAD is displaced from its binding site by NADH, Km for NADH is strongly increased
Y93A
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93D
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93F
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93H
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93S
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
Y93W
mutation preceeding the conserved motif RxYTSxxSN, FAD is bound in 1:1 cofactor:protein stoichiometry
H49A
-
reduced kcat
H49E
-
elevated Km value for cytochrome b5, strongly reduced kcat
H49K
-
reduced Km value for cytochrome b5
H49Y
-
similar to wild-type
K97A
-
mutation in flavin-binding motif
K97R
-
mutation in flavin-binding motif
P247A
P247L
P248A
P248L
P249A
P249L
R63A
-
mutation in flavin-binding motif
R63K
-
mutation in flavin-binding motif
R63Q
-
mutation in flavin-binding motif
S99A
-
mutation in flavin-binding motif
S99T
-
mutation in flavin-binding motif
S99V
-
mutation in flavin-binding motif
T66A
Km for NADH is not affected, Km for cytochrome b5 is significantly enhanced
T66S
Km for NADH is not affected
T66V
turnover is reduced to 10% of the native enzyme, Km for NADH is not affected, Km for cytochrome b5 is significantly enhanced
Y65A
-
mutation in flavin-binding motif
Y65F
-
mutation in flavin-binding motif
additional information