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6.4.1.2: acetyl-CoA carboxylase

This is an abbreviated version!
For detailed information about acetyl-CoA carboxylase, go to the full flat file.

Word Map on EC 6.4.1.2

Reaction

ATP
+
acetyl-CoA
+
hydrogencarbonate
=
ADP
+
phosphate
+
malonyl-CoA

Synonyms

ACACA, ACACB, ACC, ACC-1, ACC-2, ACC1, Acc1a, Acc1b, Acc1p, ACC2, AccA, ACCalpha, ACCase, ACCase 1, ACCB, AccC, Acetyl CoA carboxylase, Acetyl coenzyme A carboxylase, acetyl coenzyme A carboxylase alpha, acetyl-CoA carboxylase, acetyl-CoA carboxylase 1, acetyl-CoA carboxylase 2, acetyl-CoA carboxylase A, acetyl-CoA carboxylase alpha, acetyl-CoA carboxylase B, acetyl-CoA carboxylase-2, acetyl-CoA carboxylase-alpha, acetyl-CoA-carboxylase, acetyl-CoA/propionyl-CoA carboxylase, Acetyl-coenzyme A carboxylase, acetyl-coenzyme-A carboxylase, acetylCoA carboxylase, acyl coenzyme A carboxylase, acyl-CoA carboxylase, BCCP1, BCCP2, CAC1A, CAC1B, Carboxylase, acetyl coenzyme A, Hfa1p, More, PccB

ECTree

     6 Ligases
         6.4 Forming carbon-carbon bonds
             6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date)
                6.4.1.2 acetyl-CoA carboxylase

Engineering

Engineering on EC 6.4.1.2 - acetyl-CoA carboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D2078G
-
naturally occuring mutation that confers resistance to ACCase inhibitors fenoxaprop, clodinafop, haloxyfop, cycloxydim, clethodim
G2096A
-
naturally occuring mutation that confers resistance to ACCase inhibitors fenoxaprop, clodinafop and haloxyfop, and probably also to clethodim
I1781L
-
naturally occuring mutation that confers resistance to ACCase inhibitors fenoxaprop, clodinafop and haloxyfop, and to cycloxydim, and probably also to clethodim
I1781L/W2027C/I2041N/D2078G/G2096A
-
naturally occuring mutant ACCase isoforms in Alopecurus myosuroides show resistance to five ACCase inhibitors, i.e. fenoxaprop, clodinafop, haloxyfop, cycloxydim, clethodim, phenotypes, overview
I2041N
-
naturally occuring mutation that confers resistance to ACCase inhibitors fenoxaprop, clodinafop and haloxyfop
W2027C
-
naturally occuring mutation that confers resistance to ACCase inhibitors fenoxaprop, clodinafop and haloxyfop
G199S
-
construction and isolation of a mutant strain less sensitive to moiramide B derivative cpd2 compared to the wild-type strain
C5493T
the single nucleotide polymorphism is associated with fat yield but not with a structural change in the enzyme
S1263A
-
site-directed mutagenesis
C2088A
-
mutation endowing clethodim resistance
D2078G
-
mutation endowing clethodim resistance
I1781L
K73E
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
K73R
the mutant shows resistance to soraphen A
L1705I
site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme
L1705I/V1967I
P1760S/I1762L/M1765V/E1919Q/P1920A/H1925F/Q2028E/M2030T/G2032E
humanized mutant of yeast CT domain is generated by replacing nine active site residues of yeast CT domain with corresponding human ACC2 CT domain residues. This humanized yeast CT domain (yCT-H9) exhibits an inhibitor sensitivity profile similar to that of human ACC while maintaining high recombinant expression yields and robust crystallizability
Q608
mutation has little effect on catalysis
R656E
mutation has little effect on catalysis
R76E
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
S1157A
-
mutation in potential site of phosphorylation, results in 9fold higher specific activity following glucose depletion
V1967I
site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme
W487A
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
G196S
-
construction and isolation of a mutant strain less sensitive to moiramide B derivative (E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide compared to the wild-type strain
I420D
-
site-directed mutagenesis of AccB, exchange of a single amino acid results in interconversion of substrate specificity of acetyl-CoA carboxylase ACC and propionyl-CoA carboxylase, PCC, EC 6.4.1.3, thus the mutant enzyme does not utilize acetyl-CoA as a substrate, but propionyl-CoA
additional information