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1.14.11.2: procollagen-proline 4-dioxygenase

This is an abbreviated version!
For detailed information about procollagen-proline 4-dioxygenase, go to the full flat file.

Word Map on EC 1.14.11.2

Reaction

Procollagen L-proline
+
2-oxoglutarate
 +
O2
=
procollagen trans-4-hydroxy-L-proline
 +
succinate
 +
CO2

Synonyms

A085R, alpha (I) subunit, anthrax-P4H, AT-P4H-1, At-P4H-2, BaP4H, C-P4H, C-P4H alpha subunit (III), C-P4H alpha(I), C-P4H alpha(III), CePHY-1/PHY-2/PDI2, collagen proline hydroxylase, collagen prolyl 4-hydroxylase, collagen prolyl 4-hydroxylase (type-II), collagen prolyl 4-hydroxylase 1, collagen prolyl-4-hydroxylase, collagen prolyl-4-hydroxylase alpha subunit 2, CP4H, CP4H1, CrP4H-1, DmP4H, egg-laying abnormal-9 prolyl hydroxylase, Egl nine homolog, EGLN, EGLN prolyl hydroxylase, EGLN3, EGLN3 hydroxylase, GBAA_4459, HIF prolyl hydroxylase, HIF prolyl-4-hydroxylase, HIF-1alpha-specific prolyl-hydroxylase, HIF-P4H-1, HIF-P4H-2, HIF-P4H-3, HPH, HPH-2, HuPH4-I, HuPH4-II, hydroxylase, collagen proline, hypoxia inducible factor prolyl-4-hydroxylase domain-containing protein, hypoxia inducible factor-prolyl hydroxylase, hypoxia-inducible factor -1alpha-type prolyl 4-hydroxylase, hypoxia-inducible factor prolyl hydroxylase, hypoxia-inducible factor-1alpha-prolyl-hydroxylase 2, More, NtP4H1.1, P4H, P4H alpha1, P4H-1, P4H1, P4ha1, P4ha2, P4Halpha(I), P4Halpha(II), P4Halpha(III), P4Halpha1, PBCV-1 P4H, peptidyl proline hydroxylase, PH, PHD, PHD-1, PHD1, PHD2, PHD3, procollagen prolyl 4-hydroxylase, procollagen-proline dioxygenase, proline 4-hydroxylase, proline hydroxylase, proline protocollagen hydroxylase, proline, 2-oxoglutarate dioxygenase, proline,2-oxoglutarate 4-dioxygenase, prolyl 4-hydroxylase, prolyl 4-hydroxylase A085R, prolyl hydroxylase, prolyl hydroxylase domain 1, prolyl hydroxylase domain containing protein, prolyl hydroxylase domain enzyme, prolyl hydroxylase domain protein 2, prolyl hydroxylase-1, prolyl hydroxylase-3, prolyl-4-hydroxylase, prolyl-4-hydroxylase alpha I, prolyl-4-hydroxylase alpha II, prolyl-4-hydroxylase alpha subunit 2, prolyl-4-hydroxylase alpha1, prolyl-4-hydroxylase-alpha1, prolyl-4-hydroxylases, prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, 4-hydroxylating, prolyl4-hydroxylase, prolylprotocollagen dioxygenase, prolylprotocollagen hydroxylase, protocollagen hydroxylase, protocollagen proline 4-hydroxylase, protocollagen proline dioxygenase, protocollagen proline hydroxylase, protocollagen prolyl hydroxylase, PSB-II, Skp1 prolyl hydroxylase, type I C-P4H, type I proly 4-hydroxylase, type I proyl 4-hydroxylase, type II proyl 4-hydroxylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.2 procollagen-proline 4-dioxygenase

Engineering

Engineering on EC 1.14.11.2 - procollagen-proline 4-dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H180A
the mutation completely inactivates the enzyme
H180Q
the mutation completely inactivates the enzyme
H260A
the mutation completely inactivates the enzyme
H260Q
the mutation completely inactivates the enzyme
K270A
the mutation completely inactivates the enzyme
K270R
the mutation completely inactivates the enzyme
N182A
the mutation completely inactivates the enzyme
N182Q
the mutation completely inactivates the enzyme
R278A
the mutation completely inactivates the enzyme
R278H
the mutation reduces the enzyme activity to approximately 26%
S272A
the mutation reduces the enzyme activity by 83%
D405
-
inactivation of catalytic site in PHY-2 subunit, 8% of wild-type PHY-1/PHY-2/(PDI-2)2 P4H tetramer activity
D407N
-
inactivation of catalytic site in PHY-1 subunit, 5% of wild-type PHY-1/PHY-2/(PDI-2)2 P4H tetramer activity
L484A
-
lysine of PHY-2 that binds the C-5 carboxyl group of 2-oxoglutarate, 27% of wild-type PHY-1/PHY-2/(PDI-2)2 P4H tetramer activity
L486A
-
lysine of PHY-1 that binds the C-5 carboxyl group of 2-oxoglutarate, 25% of wild-type PHY-1/PHY-2/(PDI-2)2 P4H tetramer activity
D149A
-
a mutation at the tip of the betaII-betaIII loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
D149N
-
a mutation at the tip of the betaII-betaIII loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
D81A
-
a mutation at the tip of the beta3-beta4 loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
E127A
-
very low catalytic activity
G85A
-
a mutation at the tip of the beta3-beta4 loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
H245A
-
no catalytic activity
N152A
-
a mutation at the tip of the betaII-betaIII loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
Q130A
-
almost 2-fold increase in Km for poly(L-Pro)
R161A
-
no catalytic activity
R93A
-
no catalytic activity
S78T
-
a mutation at the entrance and exit of the beta3-beta4 loop, the mutant shows slightly reduced activity compared to the wild-type enzyme
S78T/S87L
-
a mutation at the entrance and exit of the beta3-beta4 loop, the mutant shows slightly reduced activity compared to the wild-type enzyme
S84A
-
a mutation at the tip of the beta3-beta4 loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
S87L
-
a mutation at the entrance and exit of the beta3-beta4 loop, the mutant shows slightly reduced activity compared to the wild-type enzyme
S95A
-
no catalytic activity
W243A
-
Km values similar to wild-type, 10-fold decrease in kcat
W99A
-
2.5-fold increase in Km for poly(L-Pro)
Y134F
-
6-fold increase in Km for 2-oxoglutarate, decrease in kcat
Y140A
-
no catalytic activity
Y140F
-
a mutation at the betaI-betaII loop, the mutant shows reduced activity and narrower substrate specificity due to altered substrate binding compared to the wild-type enzyme
Y168F
-
3-4-fold increase in Km for 2-oxoglutarate, decrease in kcat
R490H
-
the mutation reduces the percentage of uncoupled decarboxylation
R490S
-
the mutation increases the Km for 2-oxoglutarate, reduces the reaction velocity and increases the percentage of uncoupled decarboxylation
C150S
-
the mutation has no major effect on tetramer assembly, but the amount of tetramer is slightly reduced, being about 80% of that of the wild-type enzyme
C486S
-
the mutation totally prevents tetramer assembly
C511S
-
the mutation totally prevents tetramer assembly
D414A
-
site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive
D414G
-
site-directed mutagenesis, the mutation mimics the active site of a halogenase. The substitutions does not convert P4H into a halogenase, but the hydroxylase activity of D414A P4H cannot be rescued with small molecule, the mutant is inactive
D414H
-
site-directed mutagenesis, the mutation mimics the active site of a cysteine dioxygenase, the mutant is inactive
D414H/H483D
-
site-directed mutagenesis, the mutant is inactive
H131A/D315A
-
inactive mutant
H141S
-
the mutation has no effect on enzyme activity and does not inhibit tetramer assembly
H165S
-
the mutation produces a reduction of about 60% in enzyme activity per unit extractable cell protein relative to that obtained with the wild-type alpha subunit, the amount of tetramer is reduced by about 20-25%, the Km values for Fe2+, 2-oxoglutarate, ascorbate and the peptide substrate with the mutant are identical to those with the wild-type enzyme
H221S
-
the mutation produces a reduction of about 30% in enzyme activity per unit extractable cell protein relative to that obtained with the wild-type alpha subunit, the amount of tetramer is reduced by about 20-25%, the Km values for Fe2+, 2-oxoglutarate, ascorbate and the peptide substrate with the mutant are identical to those with the wild-type enzyme
H296S
-
the mutation has no effect on enzyme activity and does not inhibit tetramer assembly
H324S
-
the mutation totally prevents tetramer assembly
H412D/D414H
-
site-directed mutagenesis, the mutant is inactive
H412S
-
the mutation causes a complete inactivation of the enzyme with no effect on tetramer assembly or binding of the tetramer to poly(L-proline), role in the binding of Fe2+ to a catalytic site
H483S
-
the mutation causes a complete inactivation of the enzyme with no effect on tetramer assembly or binding of the tetramer to poly(L-proline), role in the binding of Fe2+ to a catalytic site
H501S
-
the mutation reduces the enzyme activity to about 4% with no effect on tetramer assembly or binding of the tetramer to poly(L-proline), role in the binding of Fe2+ to a catalytic site, the Km values for Fe2+, ascorbate and the peptide substrate with the mutant are identical to those with the wild-type enzyme, but the Km for 2-oxoglutarate is about 2.5fold higher. The main difference is that the Vmax determined from kinetic plots is consistently less than about 5% of that of the wild-type enzyme
H63S
-
the mutation has no effect on enzyme activity and does not inhibit tetramer assembly
N96Q/N242Q
-
the amount of enzyme activity observed with the double mutant alpha subunit is identical to that of the wild-type enzyme, the size of the double mutant alpha subunit is distinctly smaller than that of either the diglycosylated or monoglycosylated alpha subunit present in the wild-type enzyme, the difference being consistent with loss of all the carbohydrate
P191A
-
loss of hypoxic inducibility
P317R
-
naturally occuring mutation, near the Fe2+ binding site, causing erythrocytosis
R367K
no activity
R371H
-
naturally occuring mutation causing erythrocytosis
W243F
site-directed mutagenesis, mutant structure analysis compared to the wild-type enzyme, the substrate reaches equilibrium within 10 ns. Replacement of Trp243 by Phe increases the accessibility to the oxidant
W243G
site-directed mutagenesis, mutant structure analysis compared to the wild-type enzyme, the substrate equilibrium is not reached after 10 ns
Y140F
site-directed mutagenesis, mutant structure analysis compared to the wild-type enzyme, the substrate reaches equilibrium within 10 ns, inactive mutant
Y140G
site-directed mutagenesis, mutant structure analysis compared to the wild-type enzyme, the substrate reaches equilibrium within 10 ns
Y140G/W243G
site-directed mutagenesis, mutant structure analysis compared to the wild-type enzyme, the substrate equilibrium is not reached after 10 ns. The Y140G/W243G double mutant shows the accumulative effect of both the Y140G and W243G mutations
H196R
-
inactive mutant
additional information