BRENDA - Enzyme Database show
show all sequences of 1.14.11.6

Molecular basis for the substrate specificity and catalytic mechanism of thymine-7-hydroxylase in fungi

Li, W.; Zhang, T.; Ding, J.; Nucleic Acids Res. 43, 10026-10038 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Codon Plus
Neurospora crassa
Crystallization (Commentary)
Crystallization
Organism
purified recombinant full-length or truncated enzyme (unmodified or SeMet-labeled) in apo form, or complexed with 2-oxoglutarate, thymine, 5-hydroxymethyluracil, or 5-formyluracil, drop vapour diffusion method, 16C, the reservoir solution consists of 0.2 M (NH4)2SO4, 0.1 M MES, pH 6.5, and 30% w/v PEGMME 5000 for the apoenzyme, for the 2-oxoglutarate complexed enzyme of 0.1 M bis-Tris, pH 5.5, and 25% w/v PEG 3,350, and 2-oxoglutarate in a 1:4 ratio protein/2-OG, or for enzyme in complex with other ligands in a 1:4:8 ratio, X-ray diffraction structure determination and analysis at 2.05-2.43 A resolution
Neurospora crassa
Engineering
Amino acid exchange
Commentary
Organism
D216N
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
E122A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
F292A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Neurospora crassa
H214A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
H271A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Neurospora crassa
L192A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
L223A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
additional information
construction of a C-terminally truncated enzyme mutant NcT7H, comprising residues 1-299
Neurospora crassa
N294A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
Neurospora crassa
N87A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R190A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R190K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R286A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R286K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
S288A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
V273A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
Y194F
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
Y217A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Neurospora crassa
Y217F
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Neurospora crassa
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ni2+
binding structure with truncated enzyme mutant
Neurospora crassa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics, isothermal titration calorimetry analysis, steady-state kinetics of enzyme mutants, overview
Neurospora crassa
0.141
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.178
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.253
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on, required for catalysis
Neurospora crassa
additional information
Ni2+ and Ca2+ cannot substitute for Fe2+, binding structure with truncated enzyme mutant. Residues His214, Asp216 and His271 play essential roles in the metal ion binding
Neurospora crassa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-carboxyluracil + O2
Neurospora crassa
-
?
-
-
?
5-formyluracil + O2
Neurospora crassa
-
?
-
-
?
thymine + 2-oxoglutarate + O2
Neurospora crassa
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Neurospora crassa
Q7RYZ9
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Condon Plus by nickel affinity chromatography and gel filtration
Neurospora crassa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-carboxyluracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
5-formyluracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
5-hydroxyuracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
thymine + 2-oxoglutarate + O2
-
745921
Neurospora crassa
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
thymine + 2-oxoglutarate + O2
i.e. 5-methyluracil
745921
Neurospora crassa
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
enzyme structure analysis, overview
Neurospora crassa
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
37
assay at
Neurospora crassa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.325
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.416
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.765
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Neurospora crassa
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Codon Plus
Neurospora crassa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant full-length or truncated enzyme (unmodified or SeMet-labeled) in apo form, or complexed with 2-oxoglutarate, thymine, 5-hydroxymethyluracil, or 5-formyluracil, drop vapour diffusion method, 16C, the reservoir solution consists of 0.2 M (NH4)2SO4, 0.1 M MES, pH 6.5, and 30% w/v PEGMME 5000 for the apoenzyme, for the 2-oxoglutarate complexed enzyme of 0.1 M bis-Tris, pH 5.5, and 25% w/v PEG 3,350, and 2-oxoglutarate in a 1:4 ratio protein/2-OG, or for enzyme in complex with other ligands in a 1:4:8 ratio, X-ray diffraction structure determination and analysis at 2.05-2.43 A resolution
Neurospora crassa
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D216N
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
E122A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
F292A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Neurospora crassa
H214A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
H271A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Neurospora crassa
L192A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
L223A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
additional information
construction of a C-terminally truncated enzyme mutant NcT7H, comprising residues 1-299
Neurospora crassa
N294A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
Neurospora crassa
N87A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R190A
site-directed mutagenesis, the mutant shows highly reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R190K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R286A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
R286K
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
S288A
site-directed mutagenesis, the mutant shows similar activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
V273A
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
Y194F
site-directed mutagenesis, the mutant shows reduced activity with thymine and altered substrate specificity compared to the wild-type enzyme
Neurospora crassa
Y217A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Neurospora crassa
Y217F
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Neurospora crassa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ni2+
binding structure with truncated enzyme mutant
Neurospora crassa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics, isothermal titration calorimetry analysis, steady-state kinetics of enzyme mutants, overview
Neurospora crassa
0.141
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.178
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.253
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on, required for catalysis
Neurospora crassa
additional information
Ni2+ and Ca2+ cannot substitute for Fe2+, binding structure with truncated enzyme mutant. Residues His214, Asp216 and His271 play essential roles in the metal ion binding
Neurospora crassa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-carboxyluracil + O2
Neurospora crassa
-
?
-
-
?
5-formyluracil + O2
Neurospora crassa
-
?
-
-
?
thymine + 2-oxoglutarate + O2
Neurospora crassa
-
5-hydroxymethyluracil + succinate + CO2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Condon Plus by nickel affinity chromatography and gel filtration
Neurospora crassa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-carboxyluracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
5-formyluracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
5-hydroxyuracil + O2
-
745921
Neurospora crassa
?
-
-
-
?
thymine + 2-oxoglutarate + O2
-
745921
Neurospora crassa
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
thymine + 2-oxoglutarate + O2
i.e. 5-methyluracil
745921
Neurospora crassa
5-hydroxymethyluracil + succinate + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
enzyme structure analysis, overview
Neurospora crassa
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
37
assay at
Neurospora crassa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.325
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.416
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
0.765
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Neurospora crassa
General Information
General Information
Commentary
Organism
additional information
molecular basis for substrate specificity and catalytic mechanism of the enzyme and molecular mechanism of substrate recognition, overview. Residues Phe292, Tyr217 and Arg190 play critical roles in substrate binding and catalysis, and the interactions of the C5 modification group of substrates with the cosubstrate and enzyme contribute to the slightly varied binding affinity and activity towards different substrates. After the catalysis, the products are released and new cosubstrate and substrate are reloaded to conduct the next oxidation reaction. Active site structure, and 2-oxoglutarate binding structure, binding affinity of the enzyme for different substrates, overview. Residue Arg286 plays an important role in the binding of 2-oxoglutarate, Arg190 plays a vital role in the binding of both 2-oxoglutarate and the substrate, and Phe292 and Tyr217 play critical roles in the substrate binding
Neurospora crassa
General Information (protein specific)
General Information
Commentary
Organism
additional information
molecular basis for substrate specificity and catalytic mechanism of the enzyme and molecular mechanism of substrate recognition, overview. Residues Phe292, Tyr217 and Arg190 play critical roles in substrate binding and catalysis, and the interactions of the C5 modification group of substrates with the cosubstrate and enzyme contribute to the slightly varied binding affinity and activity towards different substrates. After the catalysis, the products are released and new cosubstrate and substrate are reloaded to conduct the next oxidation reaction. Active site structure, and 2-oxoglutarate binding structure, binding affinity of the enzyme for different substrates, overview. Residue Arg286 plays an important role in the binding of 2-oxoglutarate, Arg190 plays a vital role in the binding of both 2-oxoglutarate and the substrate, and Phe292 and Tyr217 play critical roles in the substrate binding
Neurospora crassa
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.826
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
2.404
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
3.024
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1.826
-
5-Hydroxyuracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
2.404
-
thymine
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
3.024
-
5-Formyluracil
recombinant wild-type enzyme, pH 7.5, 25C
Neurospora crassa
Other publictions for EC 1.14.11.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745735
Bullard
Base J glucosyltransferase do ...
Leishmania major
Mol. Biochem. Parasitol.
204
77-80
2015
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
745921
Li
Molecular basis for the subst ...
Neurospora crassa
Nucleic Acids Res.
43
10026-10038
2015
-
-
1
1
19
-
1
4
-
2
-
3
-
4
-
-
1
-
-
-
-
-
5
1
1
-
-
3
1
-
-
-
-
-
-
-
-
1
-
1
19
-
-
1
-
4
-
2
-
3
-
-
-
1
-
-
-
-
5
1
1
-
-
3
1
-
-
-
-
1
1
-
3
3
697315
Neidigh
Cloning and characterization o ...
Rhodotorula glutinis
Chem. Res. Toxicol.
22
885-893
2009
-
-
1
-
4
-
-
9
-
-
-
1
-
2
-
-
1
-
-
-
-
-
6
1
1
-
-
8
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
9
-
-
-
1
-
-
-
1
-
-
-
-
6
1
1
-
-
8
1
-
-
-
-
-
-
-
-
-
700084
Vainio
Evidence that J-binding protei ...
Leishmania tarentolae
Mol. Biochem. Parasitol.
164
157-161
2009
-
-
1
-
6
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
700501
Cliffe
JBP1 and JBP2 are two distinct ...
Trypanosoma brucei
Nucleic Acids Res.
37
1452-1462
2009
-
-
1
-
5
-
-
-
1
1
-
2
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
-
-
2
2
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689246
Yu
The protein that binds to DNA ...
Leishmania tarentolae, Trypanosoma brucei
Nucleic Acids Res.
35
2107-2115
2007
-
-
2
-
8
-
-
-
-
-
-
2
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
658220
Smiley
Genes of the thymidine salvage ...
Rhodotorula glutinis
Biochim. Biophys. Acta
1723
256-264
2005
-
-
1
-
-
-
-
-
-
-
1
1
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439133
Lai
-
Characterization of a novel, s ...
Rhodotorula glutinis
J. Am. Chem. Soc.
117
5023-5030
1995
-
-
-
-
-
-
1
-
-
1
-
3
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
3
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439134
Thornburg
Mechanism-based inactivation o ...
Rhodotorula glutinis
Biochemistry
32
14034-14042
1993
-
-
-
-
-
-
1
-
-
1
-
3
-
1
-
-
-
-
-
-
1
1
6
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
3
-
-
-
-
-
-
1
1
6
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
439135
Thornburg
A non-heme iron protein with h ...
Rhodotorula glutinis
Biochemistry
32
14023-14033
1993
-
-
-
-
-
-
2
10
-
1
-
3
-
2
-
-
1
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
10
-
1
-
3
-
-
-
1
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439136
Thornburg
Mechanism-based inhibition of ...
Rhodotorula glutinis
J. Am. Chem. Soc.
111
7632-7633
1989
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439137
Warn-Cramer
Markedly different ascorbate d ...
Rhodotorula glutinis
J. Biol. Chem.
258
10551-10557
1983
2
-
-
-
-
-
-
-
-
1
2
3
-
2
-
-
1
-
-
-
1
-
3
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
1
2
3
-
-
-
1
-
-
1
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439138
Holme
Studies on the partial reactio ...
Neurospora crassa, Neurospora crassa STA 4
Biochim. Biophys. Acta
704
278-283
1982
1
-
-
-
-
-
1
-
-
1
-
6
-
7
-
-
1
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
1
-
6
-
-
-
1
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439139
Hsu
Uracils uncoupling of the deca ...
Neurospora crassa, Neurospora crassa uc-1
J. Biol. Chem.
256
6098-6101
1981
2
-
-
-
-
-
1
2
-
1
-
2
-
3
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
1
1
2
-
1
-
2
-
-
-
-
-
1
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439140
Wondrack
Substitution of nucleoside tri ...
Rhodotorula glutinis
J. Biol. Chem.
254
26-29
1979
7
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
439141
Wondrack
Thymine 7-hydroxylase and pyri ...
Rhodotorula glutinis
J. Biol. Chem.
253
6511-6515
1978
1
-
-
-
-
-
-
-
-
1
-
3
-
2
-
-
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439142
Bankel
Thymine 7-hydroxylase from Neu ...
Neurospora crassa, Neurospora crassa STA 4
Biochim. Biophys. Acta
481
431-437
1977
-
-
-
-
-
-
16
8
-
-
-
6
-
8
-
-
-
-
-
-
-
-
15
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
16
-
8
-
-
-
6
-
-
-
-
-
-
-
-
15
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439143
Holme
A kinetic study of thymine 7-h ...
Neurospora crassa, Neurospora crassa STA 4
Biochemistry
14
4999-5003
1975
-
-
-
-
-
-
2
-
-
-
-
6
-
8
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439144
Liu
Catalysis of three sequential ...
Neurospora crassa 1A, Neurospora crassa
Arch. Biochem. Biophys.
159
180-187
1973
-
-
-
-
-
-
3
-
-
1
-
-
-
7
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
439145
Bankel
Oxygenases involved in thymine ...
Neurospora crassa, Neurospora crassa STA 4
FEBS Lett.
21
135-138
1972
-
-
-
-
-
1
-
-
-
1
-
-
-
7
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439146
McCroskey
-
Studies pertaining to the puri ...
Neurospora crassa, Neurospora crassa 1A
Biochim. Biophys. Acta
277
264-277
1971
-
-
-
-
-
-
-
-
-
1
-
2
-
7
-
-
1
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
439147
Abbott
Conversion of thymine to 5-hyd ...
Neurospora crassa, Neurospora crassa 1A
J. Biol. Chem.
239
156-159
1964
-
-
-
-
-
-
-
-
-
-
-
2
-
7
-
-
-
-
-
1
-
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-