Information on EC 1.1.1.36 - acetoacetyl-CoA reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.36
-
RECOMMENDED NAME
GeneOntology No.
acetoacetyl-CoA reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydration
-
-
oxidation
-
-
redox reaction
reduction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
-
-
acetyl-CoA fermentation to butanoate II
-
-
ethylmalonyl-CoA pathway
-
-
polyhydroxybutanoate biosynthesis
-
-
CO2 fixation in Crenarchaeota
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Butanoate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-41-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 4AK4
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
isozymes KCR1 and KCR2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
or ATCC 33960, gene fabG1
SwissProt
Manually annotated by BRENDA team
or ATCC 33960, gene fabG1
SwissProt
Manually annotated by BRENDA team
no activity in Escherichia coli
strain DH5alpha
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli DH5-alpha
strain DH5alpha
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
fox2 mutant strain
-
-
Manually annotated by BRENDA team
Streptococcus equi zooepidemicus
-
-
Manually annotated by BRENDA team
ssp. Wolfei
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
KCR catalyzes the first reduction during elongation of very-long-chain fatty acids, VLCFA, precursors of sphingolipids, triacylglycerols, cuticular waxes, and suberin in plants, but only AtKCR1 is a functional KCR isoform involved in microsomal fatty acid elongation
physiological function
-
suppressed KCR activity results in a reduction of cuticular wax load and affects VLCFA composition of sphingolipids, seed triacylglycerols, and root glycerolipids
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxydecanoyl-CoA + NADP+
3-oxodecanoyl-CoA + NADPH + H+
show the reaction diagram
-
(3R)-hydroxyacyl-CoA dehydrogenase
-
-
?
(3R)-hydroxybutyryl-CoA + NAD+
3-oxobutylryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
(3R)-hydroxybutyryl-CoA + NADP+
3-oxobutyryl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
?
(3R)-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
(3R)-hydroxyhexadecanoyl-CoA + NADP+
3-oxohexadecanoyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
show the reaction diagram
-
dehydration, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
oxidation, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxydecanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
2-methylacetoacetyl-CoA + NADPH
2-methyl-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
?
? + NADPH
(R)-3-hydroxybutyrylphosphopantetheine + NADP+
show the reaction diagram
-
-
-
?
acetoacetyl-CoA + NADH
D-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
PHA-synthesis
-
ir
acetoacetyl-CoA + NADH
D-beta-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADH
L-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADH
L-beta-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADPH
(R)-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-CoA + NADPH
?
show the reaction diagram
-
biosynthesis of poly(D-3-hydroxybutyrate)
-
-
-
acetoacetyl-CoA + NADPH
D-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-CoA + NADPH + H+
(3R)-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-S-(D-pantetheine)11-pivalate + NADPH
3-hydroxybutyryl-S-(D-pantetheine)11-pivalate + NADP+
show the reaction diagram
-
-
-
?
beta-ketopalmitoyl-CoA + ?
?
show the reaction diagram
-
-
-
?
butyrylacetyl-CoA + NADPH
3-hydroxyhexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
show the reaction diagram
D-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
show the reaction diagram
-
-
-
r
pantetheine 11-pivalate + ?
?
show the reaction diagram
-
-
-
-
?
propionylacetyl-CoA + NADPH
3-hydroxypentanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
S-acetoacetyl-N-acetylcysteamine + NADPH
3-hydroxybutyryl-N-acetylcysteamine + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxybutyryl-CoA
trans-2-butenoyl-CoA + H2O
show the reaction diagram
-
dehydration, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
oxidation, multifunctional type 2 enzyme
-
-
?
(R)-3-hydroxybutyryl-CoA + NADPH + H+
3-oxobutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADH
D-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
PHA-synthesis
-
ir
acetoacetyl-CoA + NADH
L-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADPH
(R)-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
step in the biosynthesis of polyhydroxybutyrate, a biodegradable thermoplastic polymer
-
-
?
acetoacetyl-CoA + NADPH
?
show the reaction diagram
-
biosynthesis of poly(D-3-hydroxybutyrate)
-
-
-
acetoacetyl-CoA + NADPH
D-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
acetoacetyl-CoA + NADPH + H+
(R)-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
D-3-hydroxyacyl-CoA + NAD+
3-ketoacyl-CoA + NADH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
binding mode and conformation of NAD+ bound to the enzyme derived from the crystal structure, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-methylcrotonyl-CoA
acetoacetyl-CoA
acetyl-CoA
Butyryl-CoA
iodoacetamide
malonyl-CoA
methylmalonyl-CoA
N-Methylmaleimide
N-Phenylmaleimide
NADP+
NADPH
propionylacetyl-CoA
-
-
sulfhydryl reagents
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-ketoglutarate
-
20% activation
ATP
-
32% activation
citrate
-
30% activation
isocitrate
-
25% activation, stimulates NADP+ regeneration
pantetheine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0054 - 0.0058
(3R)-3-hydroxydecanoyl-CoA
0.055
(3R)-hydroxybutyryl-CoA
-
A+/B+CtMFE-2(h2delta); A-/B+CtMFE-2(hdelta2deltaadelta)
0.024 - 0.025
(3R)-hydroxyhexadecanoyl-CoA
0.74
2-methylacetoacetyl-CoA
-
-
0.002 - 0.74
acetoacetyl-CoA
0.82
acetoacetyl-pantetheine
-
-
0.99
Acetoacetyl-S-(D-pantetheine)11-pivalate
-
-
0.006
beta-ketopalmitoyl-CoA
-
-
0.01
butyrylacetyl-CoA
-
-
0.026
D-3-hydroxybutyryl-CoA
-
-
0.03
D-beta-hydroxybutyryl-CoA
-
-
0.033
D-hydroxybutyryl-CoA
-
-
0.022
L-beta-hydroxybutyryl-CoA
-
-
0.25
NAD+
-
-
0.018 - 0.4
NADH
0.031 - 0.06
NADP+
0.018 - 0.041
NADPH
0.002
propionylacetyl-CoA
-
-
0.008 - 0.04
S-acetoacetyl-N-acetylcysteamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17 - 53
(3R)-3-hydroxydecanoyl-CoA
29 - 31
(3R)-hydroxybutyryl-CoA
3 - 41
(3R)-hydroxyhexadecanoyl-CoA
27
2-methylacetoacetyl-CoA
Zoogloea ramigera
-
-
300
acetoacetyl-CoA
Zoogloea ramigera
-
-
267
Acetoacetyl-S-(D-pantetheine)11-pivalate
Zoogloea ramigera
-
-
9
butyrylacetyl-CoA
Zoogloea ramigera
-
-
90
D-3-hydroxybutyryl-CoA
Zoogloea ramigera
-
-
124
propionylacetyl-CoA
Zoogloea ramigera
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.023
-
strain HsMFE-2(Y347A), (3R)-hydroxyacyl-CoA dehydrogenase; strain HsMFE-2(Y410A), (3R)-hydroxyacyl-CoA dehydrogenase
0.039
-
strain HsMFE-2(E408A), (3R)-hydroxyacyl-CoA dehydrogenase
0.041
-
strain HsMFE-2(D490A), (3R)-hydroxyacyl-CoA dehydrogenase
0.046
-
strain HsMFE-2(H406A), (3R)-hydroxyacyl-CoA dehydrogenase
0.047
-
strain HsMFE-2(D370A), (3R)-hydroxyacyl-CoA dehydrogenase
0.048
-
strain HsMFE-2(D517A), (3R)-hydroxyacyl-CoA dehydrogenase
0.051
-
strain HsMFE-2(D510A), (3R)-hydroxyacyl-CoA dehydrogenase
0.056
-
strain HsMFE-2(E366A), (3R)-hydroxyacyl-CoA dehydrogenase
0.066
-
strain HsMFE-2(H532A), (3R)-hydroxyacyl-CoA dehydrogenase
0.08
-
(3R)-hydroxyacyl-CoA dehydrogenase, Hs MFE-2
0.082
-
strain HsMFE-2, (3R)-hydroxyacyl-CoA dehydrogenase
0.091
-
strain UTL-7A, (3R)-hydroxyacyl-CoA dehydrogenase
0.43
-
(R)-3-hydroxybutyryl-CoA as substrate, activity of D-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-II
0.5
-
(3R)-hydroxyacyl-CoA dehydrogenase, Sc A-/B+
0.53 - 0.62
-
recombinant enzyme in transformed Escherichia coli strain DH5alpha
0.58
-
(R)-3-hydroxydecanoyl-CoA as substrate, activity of D-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-II
0.9
-
(3R)-hydroxyacyl-CoA dehydrogenase, Sc B-/A+
1.23
-
enzyme from recombinant strain, monitored at 340 nm by the depletion of NADPH during the reaction.
1.3
-
(3R)-hydroxyacyl-CoA dehydrogenase, Sc MFE-2
7.7
-
NADPH-linked
9
-
beta-ketopalmitoyl-CoA
45.2
-
acetoacetyl-CoA
87.9
Pigeon
-
fed pigeons livers
125
-
last purification step, 5.9fold purification. Candida tropicalis recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] from Escherichia coli
170.1
Pigeon
-
fasted pigeons livers
250
Pigeon
-
-
771
-
NADH-linked, 345 with NADPH
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
NADH-linked, reverse reaction pH 9.5; NADPH-linked, reverse reaction pH 10.0
7.5 - 8
-
assay at
8.1
-
reduction of acetoacetyl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
Pigeon
-
70-35% of initial acetoacetyl-CoA reduced
8
-
no activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
developing, KCR1 and KCR2
Manually annotated by BRENDA team
-
KCR1 and KCR2
Manually annotated by BRENDA team
-
KCR1 and KCR2
Manually annotated by BRENDA team
-
KCR1 and KCR2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26300
-
SDS-PAGE
76000
-
SDS-PAGE
100000
-
gel filtration
140000
-
gel-filtration
141000
-
gradient PAGE
250000
340000
-
NADH-linked: gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
crystal structure, enzyme shows a alpha/beta short chain alcohol dehydrogenase/reductase, i.e. SDR, fold
heterodimer
-
residues 1-313 and 314-604 forming the dehydrogenase A and B units, respectively
tetramer
additional information
-
the recombinant truncated and selenomethionine-labeled enzyme has a molecular weight of 34602 Da as determined by mass spectrometry
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5 mg/ml purified recombinant, detagged truncated enzyme, amino acid residues 1-604, by vapor diffusion technique, 20C, in 30% PEG 4000, 0.1 M sodium acetate, pH 4.2, 0.2 M ammonium acetate, equal volume of 0.002 ml of protein and precipitant solution, 11% v/v glycerol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.22-2.36 A resolution, the wild-type enzyme, comprising amino acid residues 1-906, is unstable and not crystallizable
-
hanging-drop vapour diffusion
-
selenomethionine-labeled recombinant truncated enzyme, X-ray diffraction structure determination and analysis at 2.38 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
-
286617
additional information
Pigeon
-
above pH 8.5 acetoacetyl-CoA not stable
286613
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes during purification
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
-
during purification
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM Tris/HCl buffer, pH 7.5, 10 mM 2-mercaptoethanol, 50% glycerol, several months
-
0C and -20C, 10 mM Tris/HCl buffer, pH 7.5, 10 mM 2-mercaptoethanol, rather unstable
-
0C, 25 mM Tris-HCl, pH 8.0
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DEAE-Sephasrose CL-6B, hydroxyapatite, Red-Sepharose CL-6B chromatography
-
ammonium sulfate fractionation, hydroxylapatite, Sephadex G-200 chromatography
-
ammonium sulfate fractionation, ion exchange, hydroxyapatite, affinity chromatography
-
Candida tropicalis recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] from Escherichia coli
-
DEAE-Sepharose chromatography, Blue gel column
-
fractionated with ammonium sulfate
Pigeon
-
gel-filtration Sephadex G-200, DEAE-cellulose chromatography, sucrose-gradient centrifugation
-
KCl extraction
-
NADH-linked: DEAE-Sepharose CL-6B, Blue Sepharose CL-6B, botyl Sepharose 4B, Mono Q 5/5; NADPH-linked: DEAE-Sepharose CL-6B, Red 120-agarose, phenyle Sepharose
-
PEG, DEAE-Toyopearl column
-
recombinant His-tagged enzyme from Escherichia coli by nickel-affinity chromatography
-
recombinant His-tagged, truncated enzyme from Escherichia coli, the His-tag is cleaved off by factor Xa
-
recombinant truncated enzyme from Escherichia coli, to homogeneity
-
Resource S cation exchange chromatography and Superdex 200 HR 10/30 column chromatography
-
the FOX2 gene is overexpressed from a multicopy vector (YEp352) in Saccharomyces cerevisiae and the gene product purified to apparent homogenity. A truncated version of MFP lacking 271 carboxyl-terminal amino acids is also overexpressed and purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the yeast expression plasmid pYE352, Saccharomyces cerevisiae fox-2 cells, devoid of Sc MFE-2, transformed with pYE352::ScMFE-2(adelta) and pYE352::ScMFE-2(bdelta). The recombinant (3R)-hydroxyacyl-CoA dehydrogenase [CiMFE-2(h2delta)] transformed into Escherichia coli
-
DNA sequence determination and analysis, construction of 5 different expression constructs for transformation of Zea mays plants, one of which contains the small subunit 24 amino acid transit peptide of Pisum sativum ribulose bisphosphate carboxylase
-
expressed in Brassica napus, transported with fusion peptide to seed leukoplast
-
expressed in Escherichia coli
-
expressed in Escherichia coli JM155
-
expressed in Escherichia coli strain JM109
-
expression of a truncated enzyme, comprising residues Met1-Asp319 of the dehydrogenase region, lacking the hydratase-2 region, in Escherichia coli
-
functional co-expression of PHA synthesis genes phaAB in Aeromonas hydrophila 4AK4 encoding beta-ketothiolase and the NADPH-dependent acetoacetyl-CoA reductase, leading to production of terpolyester poly(3-hydroxybutyrate-co-3-hydroxyvalerate-co-3-hydroxyhexanoate), addition of propionate alters the monomer composition of the polymer, overview
-
gene fabG1, DNA sequence determination and analysis, expression in the fabG1-deficient mutant, phylogenetic tree, sequence comparison of FabG1 to FabG6
gene phaB, expression of the N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene phbB, functional expression in Escherichia coli strains BW25113 and DH5alpha, co-expression with genes phbA and tesB, encoding beta-ketothiolase and thioesterase II, respectively, to reconstruct the R-3-hydroxybutyric acid production pathway, optimization of culture conditions, overview
-
gene phbB, functional expression of the phaABCRe operon containing genes phbA, phbB and phbC of the PHA biosynthetic pathway of Ralstonia eutropha, which encode beta-ketothiolase, NADPH-linked acetoacetyl-CoA reductase and PHA synthase, respectively, in Saccharomyces cerevisiae strain INVSc1/PHA1 and in non-convenient Kloeckera spp. strain KY1/PHA, reconstruction of the PHA biosynthetic pathway leading to accumulation of poly-3-hydroxybutyrate and copolymer poly-(3-hydroxybutyrate-co-poly-3-hydroxyvalerate), respectively, overview
-
isozymes KCR1 and KCR2, DNA and amino acid sequence determination, expression analysis, complementation of the yeast ybr159D mutant only isozyme KCR1, overview
-
N-terminal part of amino acids 1-604 is expressed as a C-terminally His-tagged, stable protein in Escherichia coli strain BL21(DE3)
-
wild type (HsMFE-2) and its variants are expressed in Saccharomyces cerevisiae
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A+/B+CtMFE-2(h2delta)
-
recombinant enzyme
A-/B+CtMFE-2(hdelta2deltaadelta)
-
domain A deleted
A-/B-CtMFE-2(hdelta2deltabdelta)
-
domain A and B deleted
D370A
-
site-directed mutagenesis
D490A
-
site-directed mutagenesis
D510A
-
site-directed mutagenesis, inactive
D517A
-
site-directed mutagenesis
E366A
-
site-directed mutagenesis, kcat/Km 100times lower than that of the wild type
E408A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
H406A
-
site-directed mutagenesis
H515A
-
site-directed mutagenesis
H532A
-
site-directed mutagenesis
Y347A
-
site-directed mutagenesis
Y410A
-
site-directed mutagenesis
Y505A
-
site-directed mutagenesis
G16S
-
site-directed mutagenesis
G329S
-
site-directed mutagenesis
truncated version
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
construction an evaluation of a polyhydroxybutyrate production system using Zea mays chloroplasts expressing the enzyme from Alcaligenes eutrophus
synthesis
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