BRENDA - Enzyme Database show
show all sequences of 2.3.1.39

Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase

Keatinge-Clay, A.T.; Shelat, A.A.; Savage, D.F.; Tsai, S.C.; Miercke, L.J.; O'Connell, J.D., 3rd; Khosla, C.; Stroud, R.M.; Structure 11, 147-154 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene fabD, expression of His-tagged enzyme in Escherichia coli strain BL21
Streptomyces coelicolor
Crystallization (Commentary)
Crystallization
Organism
recombinant purified enzyme, 3 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, hanging drop vapoir diffusion method, 3 days, room temperature, soaking of crystals in 30% PEG 4000, 100 mM sodium acetate, pH 4.8, 200 mM ammonium acetate, and 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0 A resolution, macromolecular docking simulation with K47A/K190A/R287A/K293A mutant actinorhodin ACP structure, overview
Streptomyces coelicolor
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
malonyl-CoA + [acyl-carrier protein]
Streptomyces coelicolor
enzyme is involved in both fatty acid and polyketide synthesis pathways
CoA + malonyl-[acyl-carrier protein]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces coelicolor
-
gene fabD
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
Streptomyces coelicolor
Reaction
Reaction
Commentary
Organism
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
catalytic mechanism, [acyl-carrier protein] binding site, residues Phe200 and Met126 are involved
Streptomyces coelicolor
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
malonyl-CoA + [acyl-carrier protein]
-
663400
Streptomyces coelicolor
CoA + malonyl-[acyl-carrier protein]
-
-
-
?
malonyl-CoA + [acyl-carrier protein]
enzyme is involved in both fatty acid and polyketide synthesis pathways
663400
Streptomyces coelicolor
CoA + malonyl-[acyl-carrier protein]
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
gene fabD, expression of His-tagged enzyme in Escherichia coli strain BL21
Streptomyces coelicolor
Crystallization (Commentary) (protein specific)
Crystallization
Organism
recombinant purified enzyme, 3 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, hanging drop vapoir diffusion method, 3 days, room temperature, soaking of crystals in 30% PEG 4000, 100 mM sodium acetate, pH 4.8, 200 mM ammonium acetate, and 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0 A resolution, macromolecular docking simulation with K47A/K190A/R287A/K293A mutant actinorhodin ACP structure, overview
Streptomyces coelicolor
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
malonyl-CoA + [acyl-carrier protein]
Streptomyces coelicolor
enzyme is involved in both fatty acid and polyketide synthesis pathways
CoA + malonyl-[acyl-carrier protein]
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
Streptomyces coelicolor
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
malonyl-CoA + [acyl-carrier protein]
-
663400
Streptomyces coelicolor
CoA + malonyl-[acyl-carrier protein]
-
-
-
?
malonyl-CoA + [acyl-carrier protein]
enzyme is involved in both fatty acid and polyketide synthesis pathways
663400
Streptomyces coelicolor
CoA + malonyl-[acyl-carrier protein]
-
-
-
?
Other publictions for EC 2.3.1.39
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)
735606
Liu
Structural and biochemical cha ...
Synechocystis sp.
Biochem. Biophys. Res. Commun.
457
398-403
2015
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1
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7
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1
1
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735381
Liu
Cloning, purification, crystal ...
Synechocystis sp.
Acta Crystallogr. Sect. F
69
1256-1259
2013
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1
1
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736175
Tian
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1
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3
1
1
3
-
-
737303
Cheng
Cloning and functional analysi ...
Schizochytrium sp., Schizochytrium sp. TIO1101
World J. Microbiol. Biotechnol.
29
959-967
2013
-
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1
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1
1
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2
2
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6
-
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1
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2
1
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1
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1
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1
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1
1
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2
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1
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2
1
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1
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1
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1
1
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-
-
719159
Zhang
Improving fatty acid productio ...
Clostridium acetobutylicum, Escherichia coli, Escherichia coli ML103, Streptomyces avermitilis, Streptomyces avermitilis MA-4680, Streptomyces coelicolor
Biotechnol. Prog.
28
60-65
2012
-
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12
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4
4
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-
720409
Sun
Functional characterizations o ...
Eimeria tenella
Mol. Biochem. Parasitol.
184
20-28
2012
-
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1
-
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1
1
1
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1
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5
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1
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1
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1
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1
1
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720468
Natarajan
Crystal structure of malonyl C ...
Xanthomonas oryzae
Mol. Cells
33
19-25
2012
-
-
1
1
-
-
-
-
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4
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701546
Hong
Cloning, purification, crystal ...
Staphylococcus aureus
Acta Crystallogr. Sect. F
66
20-22
2010
-
-
1
1
-
-
-
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4
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719494
Hong
New design platform for malony ...
Staphylococcus aureus, Streptococcus pneumoniae
FEBS Lett.
584
1240-1244
2010
-
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2
2
5
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4
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2
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2
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2
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701440
Arthur
Structure and malonyl CoA-ACP ...
Streptomyces coelicolor
ACS Chem. Biol.
4
625-636
2009
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1
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703315
Gurvitz
Physiological function of myco ...
Mycobacterium tuberculosis
Comp. Funct. Genomics
2009
836172
2009
-
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1
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1
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-
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1
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3
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705648
Misra
Catalysis and mechanism of mal ...
Escherichia coli, Plasmodium falciparum
Mol. Biosyst.
5
651-659
2009
-
-
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10
-
-
4
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4
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2
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2
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5
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10
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4
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2
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5
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5
5
701486
Jung
Cloning, expression, crystalli ...
Xanthomonas oryzae
Acta Crystallogr. Sect. F
64
1143-1145
2008
-
-
1
1
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6
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684213
Ghadbane
Structure of Mycobacterium tub ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
F63
831-835
2007
-
-
1
1
-
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6
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688366
Li
The crystal structure of MCAT ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Biol.
371
1075-1083
2007
-
-
1
1
3
-
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3
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1
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4
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1
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2
1
1
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2
1
1
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1
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689905
Zhang
Malonyl-CoA: acyl carrier prot ...
Helicobacter pylori
Protein Sci.
16
1184-1192
2007
-
-
1
1
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4
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671071
Oefner
Mapping the active site of Esc ...
Escherichia coli
Acta Crystallogr. Sect. D
D62
613-618
2006
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1
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673026
Arthur
The malonyl transferase activi ...
Streptomyces coelicolor
Chem. Biol.
13
587-596
2006
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2
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676953
Huang
Purification and characterizat ...
Mycobacterium tuberculosis
Protein Expr. Purif.
45
393-399
2006
-
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1
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5
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1
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3
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1
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659451
Zhang
Cloning, expression, and chara ...
Homo sapiens
J. Biol. Chem.
280
12422-12429
2005
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1
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1
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2
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3
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1
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1
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661956
Sinha
Role for malonyl coenzyme A:ac ...
Mycobacterium tuberculosis variant bovis
J. Antimicrob. Chemother.
53
1072-1075
2004
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1
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1
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2
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3
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2
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1
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1
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2
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-
660689
Molnos
A continuous coupled enzyme as ...
Escherichia coli K-12
Anal. Biochem.
319
171-176
2003
-
1
1
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1
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1
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1
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1
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3
-
1
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1
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1
1
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1
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1
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1
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3
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1
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1
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661061
Koppisch
Structure-based mutagenesis of ...
Streptomyces coelicolor
Biochemistry
42
11057-11064
2003
-
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1
-
13
-
-
23
-
-
-
1
-
3
-
-
1
1
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-
1
-
2
-
-
-
-
14
1
-
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-
-
-
-
-
1
-
-
13
-
-
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23
-
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