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show all sequences of 1.1.1.211

Production of two monomer structures containing medium-chain-length polyhydroxyalkanoates by beta-oxidation-impaired mutant of Pseudomonas putida KT2442

Ma, L.; Zhang, H.; Liu, Q.; Chen, J.; Zhang, J.; Chen, G.Q.; Biores. Technol. 100, 4891-4894 (2009)

Data extracted from this reference:

Application
Application
Commentary
Organism
degradation
when gene encoding 3-hydroxyacyl-CoA dehydrogenase is deleted, it is possible to produce medium-chain-length polyhydroxyalkanoates containing only two different monomer structures
Pseudomonas putida
Cloned(Commentary)
Commentary
Organism
into XbaI- and HindIII-digested pK18mobsacB, resulting in plasmid pKXZ01
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
additional information
when gene encoding 3-hydroxyacyl-CoA dehydrogenase is partially or completely deleted, the polyhydroxyalkanoate accumulated has only two different monomer structures dominated by a monomer of the same chain length as that of the fatty acids fed and another monomer two carbon atoms shorter. Disruption of the 3-hydroxyacyl-CoA dehydrogenase gene dramatically reduces conversion of S-3-OH-acyl-CoA to ketoacyl-CoA, resulting in reduced beta-oxidation flux, thus, leading to the accumulation of other intermediates including enoyl-CoA which are used by the bacteria to synthesize polyhydroxyalkanoate
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
Q88L88
-
-
Pseudomonas putida KT2442
Q88L88
-
-
Application (protein specific)
Application
Commentary
Organism
degradation
when gene encoding 3-hydroxyacyl-CoA dehydrogenase is deleted, it is possible to produce medium-chain-length polyhydroxyalkanoates containing only two different monomer structures
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
into XbaI- and HindIII-digested pK18mobsacB, resulting in plasmid pKXZ01
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
when gene encoding 3-hydroxyacyl-CoA dehydrogenase is partially or completely deleted, the polyhydroxyalkanoate accumulated has only two different monomer structures dominated by a monomer of the same chain length as that of the fatty acids fed and another monomer two carbon atoms shorter. Disruption of the 3-hydroxyacyl-CoA dehydrogenase gene dramatically reduces conversion of S-3-OH-acyl-CoA to ketoacyl-CoA, resulting in reduced beta-oxidation flux, thus, leading to the accumulation of other intermediates including enoyl-CoA which are used by the bacteria to synthesize polyhydroxyalkanoate
Pseudomonas putida
Other publictions for EC 1.1.1.211
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)
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Griffin
Mutations in long-chain 3-hydr ...
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368-374
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696790
Ma
Production of two monomer stru ...
Pseudomonas putida, Pseudomonas putida KT2442
Biores. Technol.
100
4891-4894
2009
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710865
Park
Two novel HADHB gene mutations ...
Homo sapiens
Ann. Clin. Lab. Sci.
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2009
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686162
Law
A novel functional assay for s ...
Homo sapiens
Clin. Chim. Acta
382
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Kong
No mutation was found in the a ...
Homo sapiens
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22
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670281
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Effect of optimal dietary ther ...
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86
124-133
2005
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670476
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Long-chain fatty acid oxidatio ...
Homo sapiens
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755-759
2005
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11
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656815
Jones
Effects of odd-numbered medium ...
Homo sapiens
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81
96-99
2004
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656959
Rakheja
Evidence for fatty acid oxidat ...
Homo sapiens
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23
447-450
2002
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286270
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183
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3
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486411
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2
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2
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2
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1
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2
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10
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