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show all sequences of 1.14.13.200

Crystallization and preliminary X-ray analysis of tetracenomycin A2 oxygenase: a flavoprotein hydroxylase involved in polyketide biosynthesis

Beynon, J.; Rafanan, E.R.; Shen, B.; Fisher, A.J.; Acta Crystallogr. Sect. D 56, 1647-1651 (2000)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
protein crystallizes in two different space groups, both with six monomers per asymmetric unit, resulting in large unit-cell parameters. Data from both the hexagonal and tetragonal crystal forms to 4.5 and 4.2 A resolution, respectively
Streptomyces glaucescens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces glaucescens
P39888
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Crystallization (Commentary) (protein specific)
Crystallization
Organism
protein crystallizes in two different space groups, both with six monomers per asymmetric unit, resulting in large unit-cell parameters. Data from both the hexagonal and tetragonal crystal forms to 4.5 and 4.2 A resolution, respectively
Streptomyces glaucescens
Other publictions for EC 1.14.13.200
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)
730232
Rafanan
Cloning, sequencing, and heter ...
Streptomyces olivaceus, Streptomyces olivaceus Tue2353
J. Nat. Prod.
64
444-449
2001
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2
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1
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2
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4
1
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1
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728863
Beynon
Crystallization and preliminar ...
Streptomyces glaucescens
Acta Crystallogr. Sect. D
56
1647-1651
2000
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730547
Rafanan
Triple hydroxylation of tetrac ...
Streptomyces glaucescens, Streptomyces olivaceus, Streptomyces olivaceus Tue2353
Org. Lett.
2
3225-3227
2000
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2
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4
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2
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727813
Shen
Triple hydroxylation of tetrac ...
Streptomyces glaucescens
J. Biol. Chem.
269
30726-30733
1994
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3
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5
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1
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1
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729909
Decker
Nucleotide sequences and heter ...
Streptomyces glaucescens
J. Bacteriol.
175
3876-3886
1993
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