Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + carbamoyl phosphate
ATP + carbamate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ATP + 1'-N-carboxy-D-biotin + HCO3-
ADP + phosphate + ?
-
the 1'-ureido-N position of biotin is the enzymatic site of carboxylation
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
ATP + biotin-carboxyl-carrier protein + HCO3-
?
-
the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
ATP + d-biotin + HCO3-
ADP + phosphate + carboxy-d-biotin
-
BC component of the multisubunit complex of acetyl-CoA carboxylase
-
-
?
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
GTP + biotin-carboxyl-carrier protein + HCO3-
GDP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
GTP + D-biotin + HCO3-
GDP + phosphate + carboxybiotin
-
-
-
-
?
additional information
?
-
ADP + carbamoyl phosphate
ATP + carbamate
-
biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate
carbamate rapidly decomposes into carbon dioxide and ammonia
-
?
ADP + carbamoyl phosphate
ATP + carbamate
-
biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate
-
-
r
ADP + carbamoyl phosphate
ATP + carbamate
-
biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate
carbamate rapidly decomposes into carbon dioxide and ammonia
-
?
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
-
ADP in form of MgADP-
-
-
r
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
-
ADP in form of MnADP-
-
-
r
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
-
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
also uses free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
also utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, also utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
free biotin, 8000fold lower activity than with the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein, biotin carboxylase activity of acetyl-CoA carboxylase
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
utilizes free biotin as substrate
-
-
r
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
utilizes free biotin as substrate in vitro
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
ATP in form of MgATP2-
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
utilizes free biotin as substrate
-
-
?
ATP + biotin + HCO3-
ADP + phosphate + carboxybiotin
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
mathematical modeling and numerical simulations of the kinetics of wild-type, hybrid dimers, and mutant homodimers of biotin carboxylase are performed. Numerical simulations of biotin carboxylase kinetics are the most similar to the experimental data when an oscillating active site model is used. In contrast, alternative models where the active sites are independent do not agree with the experimental data. Thus, the numerical simulations of the proposed kinetic model support the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
in Gram-negative and Gram-positive bacteria biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier protein are separate proteins
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
the biotinoyl domain interacts with the biotin-carboxyl-carrier protein, BCCP, biotin must be attached to ACC to produce a functional enzyme
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
Geotalea uraniireducens
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biotin is covalently attached to a protein called the biotin-carboxyl-carrier protein. In mammals, these proteins comprise different domains in a single polypeptide chain, biotin must be attached to ACC to produce a functional enzyme
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
BC subunit of pyruvate carboxylase, BC/active site structure
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, component of the multifunctional acetyl-CoA carboxylase, roles of Arg-338 and Lys-238 in the carboxyl transfer to biotin, Arg-338 serves to orient the carboxyphosphate intermediate for optimal carboxylation of biotin
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biotin carboxylase component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the ATP-dependent carboxylation of biotin, ordered addition of substrates with ATP binding first followed by bicarbonate and then biotin
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biotin carboxylase is one of three distinct components of acetyl-CoA carboxylase, carboxylation of the ureido ring of biotin at the N-1 position, reaction mechanism, domain structure, the biotin carboxylase B-domain moves as a result of ATP binding, enzyme structure
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
Lys-238 interacts with the gamma-phosphate group of ATP but is not involved in catalysis, BC is a subunit of acetyl-CoA carboxylase and mediates the carboxylation of enzyme-bound biotin
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, for that biotin must be deprotonated at its N1 position, mechanism for deprotonation of biotin, bicarbonate is the source of CO2, Lys-238 plays a role in the carboxylation reaction, Cys-230 and Lys-238 do not act as an acid-base pair in the deprotonation of biotin, but may be involved in ATP binding
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, two complete active sites per homodimer
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding and in catalysis orienting ATP in a conformation that allows for optimal catalysis, mechanism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the first half-reaction of the reaction catalyzed by acetyl-CoA carboxylase, the half-reaction involves the phosphorylation of bicarbonate by ATP to form a carboxyphosphate intermediate, followed by transfer of the carboxyl group to biotin to form carboxybiotin, in vivo biotin is attached to biotin-carboxyl-carrier protein, the C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein form a domain that acts as excellent substrate
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism
-
-
r
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
biotin carboxylase subunit AccA of acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
biotin carboxylase subunit AccA of acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
BC component of the multisubunit complex acetyl-CoA carboxylase, BC catalyzes the ATP-dependent carboxylation of the biotinyl moiety on biotin carboxyl carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
-
-
-
-
?
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
-
sequential mechanism, in which HCO3- is activated by ATP in a first step
-
-
?
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
-
L-biotin is completely inactive
-
?
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
-
L-biotin is completely inactive
-
-
?
ATP + D-(+)-biotin + HCO3-
ADP + phosphate + carboxybiotin
-
L-biotin is completely inactive
-
-
?
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
-
ATP in form of MnATP2-
-
-
r
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
-
ATP in form of MgATP2-
-
-
r
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate
ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine
-
ATP in form of CoATP2-
-
-
r
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
enzyme catalyzes ATP-hydrolysis in absence of biotin
-
-
?
additional information
?
-
-
enzyme catalyzes ATP-hydrolysis in absence of biotin
-
-
?
additional information
?
-
-
fatty acid synthesis
-
-
?
additional information
?
-
-
fatty acid synthesis
-
-
?
additional information
?
-
-
long-chain fatty acid synthesis
-
-
?
additional information
?
-
-
biotin carboxylase catalyzes a slow bicarbonate-dependent ATP hydrolysis reaction in the absence of biotin
-
-
?
additional information
?
-
-
in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis
-
-
?
additional information
?
-
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATP hydrolysis at a slow rate
-
-
?
additional information
?
-
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin
-
-
?
additional information
?
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
?
additional information
?
-
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
?
additional information
?
-
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
?
additional information
?
-
-
mechanism of ACC holoenzyme function, structure of the biotinoyl domain, overview. In thei BCCP, Glu 119 and Glu147 interact with the basic residues in BirA, overview
-
-
?
additional information
?
-
molecular dynamics simulations of wild-type enzyme and active-site mutant E288K, overview
-
-
?
additional information
?
-
-
molecular dynamics simulations of wild-type enzyme and active-site mutant E288K, overview
-
-
?
additional information
?
-
-
in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin
-
-
?
additional information
?
-
Geotalea uraniireducens
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
during the catalytic mechanism, the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin
-
-
?
additional information
?
-
-
during the catalytic mechanism, the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin
-
-
?
additional information
?
-
during the catalytic mechanism, the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
mechanism of ACC holoenzyme function, structure of the biotinoyl domain of isozyme ACC2, overview
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
?
additional information
?
-
-
active site structure, substrate binding and structure-function relationship analysis, overview
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
additional information
?
-
the biotin carboxylase is a subunit of the acetyl CoA carboxylase, ACCase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
ATP + biotin-carboxyl-carrier protein + HCO3-
?
-
the acetyl-CoA carboxylase catalyzes the first commited step in the biosynthesis of long chain fatty acids, the acetyl-CoA carboxylase system is composed of 3 components: 1. biotin carboxylase, 2. carboxyltransferase, 3. carboxylcarrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
additional information
?
-
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committed step in fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
Geotalea uraniireducens
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
first half reaction of the first committed step in the biosynthesis of long-chain fatty acids, in vivo the biotin substrate is attached to biotin-carboxyl-carrier protein, natural substrate
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
long-chain fatty acid synthesis, in vivo biotin is covalently attached to the biotin-carboxyl-carrier protein
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to the biotin-carboxyl-carrier protein in vivo, fatty acid synthesis
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue
-
-
?
ATP + biotin-carboxyl-carrier protein + HCO3-
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
-
-
-
?
additional information
?
-
-
BC subunit of pyruvate carboxylase, which is involved in gluconeogenesis
-
-
?
additional information
?
-
-
fatty acid synthesis
-
-
?
additional information
?
-
-
fatty acid synthesis
-
-
?
additional information
?
-
-
long-chain fatty acid synthesis
-
-
?
additional information
?
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
?
additional information
?
-
-
the reaction mechanism of the acetyl-CoA carboxylase proceeds via two half-reactions: the first half-reaction is catalyzed by biotin carboxylase, the second half-reaction is catalyzed by carboxyltransferase
-
-
?
additional information
?
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
AccA is a biotinylated protein mainly expressed in the exponential growth phase
-
-
?
additional information
?
-
-
pathway from acetyl-CoA to long-chain fatty acids, developmental regulation of enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
adenosine diphosphopyridoxal
-
ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition
biotin
-
above 300 mM, noncompetitive substrate inhibitor
CTP
less than 40% residual activity at 20 mM
ethanol
-
maximal activation, 10fold, at 15% v/v. Inactivation at 20% v/v
GTP
less than 40% residual activity at 20 mM
N-ethylmaleimide
-
pH-dependent inhibition, reacts with Lys-238
Phosphonoacetate
-
competitive inhibition versus ATP, noncompetitive versus bicarbonate
phosphonoacetate linked to the 1'-nitrogen of biotin
-
reaction intermediate analog, modest inhibition, competitive versus ATP, noncompetitive versus biotin
TTP
less than 40% residual activity at 20 mM
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
minimal inhibitory concentration above 64 microg per ml for wild-type, 16 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration 8 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
minimal inhibitory concentration above 64 microg per ml for wild-type, 8 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
-
minimal inhibitory concentration 16 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
minimal inhibitory concentration 16 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
minimal inhibitory concentration 0.125 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
-
minimal inhibitory concentration 1 microg per ml for wild-type, 0.5 microg per ml for mutant with targeted knock-out of efflux pump acrA
ADP
-
-
ATP
-
the catalytic activity can be inhibited by ATP at high concentrations
ATP
ATP shows substrate inhibition which is competitive against bicarbonate
soraphen
-
-
soraphen A
macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase
soraphen A
nanomolar inhibitor against biotin carboxylase domain of acetyl-coenzyme A carboxylase. The inhibitor may bind in the biotin carboxylase dimer interface and inhibits the biotin carboxylase activity by disrupting the oligomerization of the domain
additional information
-
no substrate inhibition by ATP
-
additional information
-
not inhibited by PLP
-
additional information
-
docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233
-
additional information
-
docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233
-
additional information
-
docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C230A
-
kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin
E211A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
E276Q
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
E288A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
E296A
50fold decrease in catalytic efficiency, crystallization data
G165V/G166V
-
the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
H209A
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
H438P
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
I437T
decrease in sensitivity to inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
K116A
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K238A
-
ATP-binding residue, mutant with much decreased activity, kinetic data
K238R
-
ATP-binding residue, mutant with much decreased activity, kinetic data
M169K
-
kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
R16E
the mutant has a 2fold loss in catalytic activity compared with the wild type enzyme. The mutation significantly destabilizes the dimer
R338A
250fold decrease in catalytic efficiency
R338Q
-
kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate
R338S
-
kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate
R366E
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
R401E
mutant enzyme shows no specific activity at 2.5 mM of enzyme and up to 800 mM of ATP
E211A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
-
E288A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
-
N290A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
-
R292A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
-
V927A/I931M/M932N/T933Q
-
site-directed mutagenesis, substitution of four amino acids in the vicinity of human MKM motif in analogy to the Escherichia coli biotinylation site
E23R
mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity, mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is 2.6fold lower than wild-type value
E23R
-
the mutant protein has a kcat value about 30% that of the wild type enzyme
E288K
-
completely inactive mutant, hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 285fold decreased activity, reduced rate of fatty acid synthesis
E288K
-
mutant with completely abolished ability to hydrolyze ATP
E288K
inactive active-site mutant
F363A
mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is identical to wild-type value
F363A
-
the mutant has approximately 84% of the wild type activity
G165V
-
site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme
G165V
-
the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
G166V
-
site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows increased Km for ATP and 100fold decreased reaction velocity compared to the wild-type enzyme
G166V
-
the mutation does not affect the maximal velocity of a partial reaction, the bicarbonate-dependent ATPase activity. Km values for ATP increases over 40fold when compared with wild-type. The maximal velocity for the biotin-dependent ATPase activity, i.e. the complete reaction, decreases over 100fold
K116Q
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K116Q
-
site-directed mutagenesis, the phosphate binding site mutant has the residue of the Staphylococcus aureus enzyme and shows a 50fold increased Km for ATP compared to the wild-type enzyme
K159Q
-
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP
K159Q
-
site-directed mutagenesis, the active site mutant has the residue of the Staphylococcus aureus enzyme and shows a 90fold higher Km for ATP compared to the wild-type enzyme
K238Q
-
ATP-binding residue, mutant with much decreased activity, kinetic data
K238Q
-
hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 94fold decreased activity, reduced rate of fatty acid synthesis
K238Q
-
kinetic data, 50fold increased Km for ATP, no formation of carboxybiotin
N290A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
N290A
-
active site mutant, negative cooperativity with respect to bicarbonate
N290A
-
hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 28fold decreased activity, reduced rate of fatty acid synthesis
R19E
mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity. kcat/Km for ATP-hydrolysis is 2.5fold lower than wild-type value
R19E
-
the mutant has about half the activity of the wild type protein
R292A
-
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data
R292A
-
hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 39fold decreased activity, reduced rate of fatty acid synthesis
R292A
-
site-directed mutagenesis, the mutant has a Km for ATP similar to the wild-type enzyme
additional information
-
identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive
additional information
accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
additional information
-
accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
additional information
-
accA disruption mutant with a reduced growth rate and reduced acetyl-CoA carboxylase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
accA gene, sequencing, expression in Escherichia coli, forms together with accB a two-gene operon
accC gene, overexpression in Escherichia coli
-
expressed in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)pLysS
-
expression of biotin carboxylase domain of acetyl-coenzyme A carboxylase in Escherichia coli
expression of biotin carboxylase domain of pyruvate carboxylase in Escherichia coli
-
expression of the His-tagged biotinoyl domain in Escherichia coli strain AVB101
-
expression of wild-type and mutant His-tagged biotinoyl domains in Escherichia coli strain AVB101
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, expression in Escherichia coli srrain BL21-AI as His-tagged enzyme
-
gene accC, expression in Escherichia coli strain BL21-AI as His-tagged enzyme
-
gene accC, overexpression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
gene encoding a protein composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein
-
overexpression in Escherichia coli JM109
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
-
expression in Escherichia coli
-
expression in Escherichia coli
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
Geotalea uraniireducens
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
gene accC, DNA and amino acid sequence determination, analysis, and comparison, phylogenetic analysis, and denaturing gradient gel electrophoresis genetic fingerprinting method development and evaluation, overview
-
overexpression in Escherichia coli JM109
-
overexpression in Escherichia coli JM109
-
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
truncated biotin carboxylase domain of acetyl-CoA carboxylase, expression in Escherichia coli
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Tipton, P.A.; Cleland, W.W.
Catalytic mechanism of biotin carboxylase: steady-state kinetic investigation
Biochemistry
27
4317-4325
1988
Escherichia coli
brenda
Guchhait, R.B.; Polakis, S.E.; Lane, M.D.
Biotin carboxylase component of acetyl-CoA carboxylase from Escherichia coli
Methods Enzymol.
35B
25-31
1975
Escherichia coli
brenda
Climent, I.; Rubio, V.
ATPase activity of biotin carboxylase provides evidence for initial activation of HCO3- by ATP in the carboxylation of biotin
Arch. Biochem. Biophys.
251
465-470
1986
Escherichia coli
brenda
Polakis, S.E.; Guchhait, R.B.; Lane, M.D.
On the possible involvement of a carbonyl phosphate intermediate in the adenosine triphosphate-dependent carboxylation of biotin
J. Biol. Chem.
247
1335-1337
1972
Escherichia coli
brenda
Polakis, S.E.; Guchhait, R.B.; Zwergel, E.E.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Studies on the mechanism of the biotin carboxylase- and carboxyltransferase-catalyzed reactions
J. Biol. Chem.
249
6657-6667
1974
Escherichia coli
brenda
Guchhait, R.B.; Polakis, S.E.; Hollis, D.; Fenselau, C.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Site of carboxylation of biotin and enzymatic reactivity of 1'-N-(ureido)-carboxybiotin derivatives
J. Biol. Chem.
24 9
6646-6656
1974
Escherichia coli
brenda
Guchhait, R.B.; Polakis, S.E.; Dimroth, P.; Stoll, E.; Moss, J.; Lane, M.D.
Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
J. Biol. Chem.
249
6633-6645
1974
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Dimroth, P.; Guchhait, R.B.; Lane, M.D.
Crystallization of biotin carboxylase, a component enzyme of the acetyl-CoA carboxylase system from Escherichia coli
Hoppe-Seyler's Z. Physiol. Chem.
352
351-354
1971
Escherichia coli
brenda
Dimroth, P.; Guchhait, R.B.; Stoll, E.; Lane, M.D.
Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase
Proc. Natl. Acad. Sci. USA
67
1353-1360
1970
Escherichia coli
brenda
Kondo, H.; Shiratsuchi, K.; Yoshimoto, T.; Masuda, T.; Kitazono, A.; Tsuru, D.; Anai, M.; Sekiguchi, M.; Tanabe, T.
Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit
Proc. Natl. Acad. Sci. USA
88
9730-9733
1991
Escherichia coli
brenda
Li, S.J.; Cronan, J.E.
The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
J. Biol. Chem.
267
855-863
1992
Escherichia coli
brenda
Waldrop, G.; Holden, H.M.; Rayment, I.
Preliminary X-ray crystallographic analysis of biotin carboxylase isolated from Escherichia coli
J. Mol. Biol.
235
367-369
1994
Escherichia coli
brenda
Norman, E.; de Smet, K.A.L.; Stoker, N.G.; Ratledge, C.; Wheeler, P.R.; Dale, J.W.
Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis
J. Bacteriol.
176
2525-2531
1994
Mycobacterium tuberculosis, Mycobacterium leprae
brenda
Waldrop, G.L.; Rayment, I.; Holden, H.M.
Three-dimensional structure of the biotin carboxylase subunit of the acetyl-CoA carboxylase
Biochemistry
33
10249-10256
1994
Escherichia coli
brenda
Sun, J.; Ke, J.; Johnson, J.L.; Nikolau, B.J.; Wurtele, E.S.
Biochemical and molecular biological characterization of CAC2, the Arabidopsis thaliana gene coding for the biotin carboxylase subunit of the plastidic acetyl-coenzyme A carboxylase
Plant Physiol.
115
1371-1383
1997
Arabidopsis thaliana
brenda
Bao, X.; Shorrosh, B.S.; Ohlrogge, J.B.
Isolation and characterization of an Arabidopsis biotin carboxylase gene and its promoter
Plant Mol. Biol.
35
539-550
1997
Arabidopsis thaliana
brenda
Shintani, D.; Roesler, K.; Shorrosh, B.; Savage, L.; Ohlrogge, J.
Antisense expression and overexpression of biotin carboxylase in tobacco leaves
Plant Physiol.
114
881-886
1997
Nicotiana tabacum
brenda
Jager, W.; Peters-Wendisch, P.G.; Kalinowski, J.; Puhler, A.
A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins
Arch. Microbiol.
166
76-82
1996
Corynebacterium glutamicum
brenda
Marini, P.; Li, S.J.; Gardiol, D.; Cronan, J.E.; de Mendoza, D.
The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis
J. Bacteriol.
177
7003-7006
1995
Bacillus subtilis
brenda
Elborough, K.M.; Swinhoe, R.; Winz, R.; Kroon, J.T.; Farnsworth, L.; Fawcett, T.; Martinez-Rivas, J.M.; Slabas, A.R.
Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase: assignment of the domain structure ina full-length Arabidopsis thaliana genomuic clone
Biochem. J.
301
599-605
1994
Brassica napus
brenda
Best, E.A.; Knauf, V.C.
Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase
J. Bacteriol.
175
6881-6889
1993
Pseudomonas aeruginosa
brenda
Shorrosh, B.S.; Roesler, K.R.; Shintani, D.; van de Loo, F.J.; Ohlrogge, J.B.
Structural analysis, plastid localization, and expression of the biotin carboxylase subunit of acetyl-coenzyme A carboxylase from tobacco
Plant Physiol.
108
805-812
1995
Ricinus communis, Medicago sativa, Nicotiana tabacum, Pisum sativum
brenda
Sueda, S.; Islam, M.N.; Kondo, H.
Protein engineering of pyruvate carboxylase
Eur. J. Biochem.
271
1391-1400
2004
Geobacillus thermodenitrificans
brenda
Kimura, Y.; Miyake, R.; Tokumasu, Y.; Sato, M.
Molecular cloning and characterization of two genes for the biotin carboxylase and carboxyltransferase subunits of acetyl coenzyme A carboxylase in Myxococcus xanthus
J. Bacteriol.
182
5462-5469
2000
Myxococcus xanthus (Q9FAF5), Myxococcus xanthus, Myxococcus xanthus IFO13542 / ATCC 25232 (Q9FAF5)
brenda
Kondo, S.; Nakajima, Y.; Sugio, S.; Yong-Biao, J.; Sueda, S.; Kondo, H.
Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution
Acta Crystallogr. Sect. D
60
486-492
2004
Aquifex aeolicus
brenda
Thelen, J.J.; Ohlrogge, J.B.
The multisubunit acetyl-CoA carboxylase is strongly associated with the chloroplast envelope through non-ionic interactions to the carboxyltransferase subunits
Arch. Biochem. Biophys.
400
245-257
2002
Pisum sativum
brenda
Blanchard, C.Z.; Amspacher, D.; Strongin, R.; Waldrop, G.L.
Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism
Biochem. Biophys. Res. Commun.
266
466-471
1999
Escherichia coli
brenda
Blanchard, C.Z.; Lee, Y.M.; Frantom, P.A.; Waldrop, G.L.
Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin
Biochemistry
38
3393-3400
1999
Escherichia coli, Escherichia coli JM109
brenda
Levert, K.L.; Lloyd, R.B.; Waldrop, G.L.
Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?
Biochemistry
39
4122-4128
2000
Escherichia coli
brenda
Kazuta, Y.; Tokunaga, E.; Aramaki, E.; Kondo, H.
Identification of lysine-238 of Escherichia coli biotin carboxylase as an ATP-binding residue
FEBS Lett.
427
377-380
1998
Escherichia coli
brenda
Blanchard, C.Z.; Chapman-Smith, A.; Wallace, J.C.; Waldrop, G.L.
The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin
J. Biol. Chem.
274
31767-31769
1999
Escherichia coli
brenda
Thoden, J.B.; Blanchard, C.Z.; Holden, H.M.; Waldrop, G.L.
Movement of the biotin carboxylase B-domain as a result of ATP binding
J. Biol. Chem.
275
16183-16190
2000
Escherichia coli
brenda
Sloane, V.; Blanchard, C.Z.; Guillot, F.; Waldrop, G.L.
Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis
J. Biol. Chem.
276
24991-24996
2001
Escherichia coli
brenda
Janiyani, K.; Bordelon, T.; Waldrop, G.L.; Cronan, J.E., Jr.
Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer
J. Biol. Chem.
276
29864-29870
2001
Escherichia coli
brenda
Sloane, V.; Waldrop, G.L.
Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase
J. Biol. Chem.
279
15772-15778
2004
Escherichia coli
brenda
Weatherly, S.C.; Volrath, S.L.; Elich, T.D.
Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain
Biochem. J.
380
105-110
2004
Pyricularia grisea, Phytophthora infestans, Ustilago maydis
brenda
Shen, Y.; Volrath, S.L.; Weatherly, S.C.; Elich, T.D.; Tong, L.
A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
Mol. Cell
16
881-891
2004
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
brenda
Kondo, S.; Nakajima, Y.; Sugio, S.; Sueda, S.; Islam, M.N.; Kondo, H.
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans
Acta Crystallogr. Sect. D
63
885-890
2007
Geobacillus thermodenitrificans
brenda
de Queiroz, M.S.; Waldrop, G.L.
Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity
J. Theor. Biol.
246
167-175
2007
Escherichia coli
brenda
Shen, Y.; Chou, C.Y.; Chang, G.G.; Tong, L.
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
Mol. Cell
22
807-818
2006
Escherichia coli (P24182), Escherichia coli
brenda
Burton, N.P.; Williams, T.D.; Norris, P.R.
Carboxylase genes of Sulfolobus metallicus
Arch. Microbiol.
172
349-353
1999
Sulfuracidifex metallicus (O52602), Sulfuracidifex metallicus
brenda
Auguet, J.C.; Borrego, C.M.; Baneras, L.; Casamayor, E.O.
Fingerprinting the genetic diversity of the biotin carboxylase gene (accC) in aquatic ecosystems as a potential marker for studies of carbon dioxide assimilation in the dark
Environ. Microbiol.
10
2527-2536
2008
Chlorobium limicola, Cupriavidus metallidurans, Cytophaga hutchinsonii, Chlorobium phaeobacteroides, Methanosarcinales, Methanococcales, Sulfurisphaera tokodaii, Natronomonas pharaonis (A0A1U7EYC1), Cenarchaeum symbiosum (A0RY62), Pelobacter propionicus (A1ANN6), Hyperthermus butylicus (A2BLY3), Maribacter sp. HTCC2170 (A4APF1), Polynucleobacter asymbioticus QLW-P1DMWA-1 (A4SVB6), Geotalea uraniireducens (A5G5L1), Nitrosopumilus maritimus (A9A3E8), Chloroflexus aurantiacus (A9W9X0), uncultured bacterium (B1GX36), Sulfuracidifex metallicus (O52602), Trichodesmium erythraeum (Q10YA8), Polaromonas sp. (Q12EJ0), Syntrophotalea carbinolica (Q3A2P1), Synechococcus sp. (Q54755), Acidianus brierleyi (Q877I5), Metallosphaera sedula (Q8J2Z4), Saccharolobus solfataricus (Q97V46), Halobacterium salinarum (Q9HPP8)
brenda
Nilsson Lill, S.O.; Gao, J.; Waldrop, G.L.
Molecular dynamics simulations of biotin carboxylase
J. Phys. Chem. B
112
3149-3156
2008
Escherichia coli (P24182), Escherichia coli
brenda
Mochalkin, I.; Miller, J.R.; Evdokimov, A.; Lightle, S.; Yan, C.; Stover, C.K.; Waldrop, G.L.
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase
Protein Sci.
17
1706-1718
2008
Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Staphylococcus aureus Mu50
brenda
Lee, C.K.; Cheong, H.K.; Ryu, K.S.; Lee, J.I.; Lee, W.; Jeon, Y.H.; Cheong, C.
Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism
Proteins
72
613-624
2008
Escherichia coli, Homo sapiens
brenda
Mochalkin, I.; Miller, J.R.; Narasimhan, L.; Thanabal, V.; Erdman, P.; Cox, P.B.; Prasad, J.V.; Lightle, S.; Huband, M.D.; Stover, C.K.
Discovery of antibacterial biotin carboxylase inhibitors by virtual screening and fragment-based approaches
ACS Chem. Biol.
4
473-483
2009
Moraxella catarrhalis, Haemophilus influenzae, Escherichia coli (P24182)
brenda
Cho, Y.S.; Lee, J.I.; Shin, D.; Kim, H.T.; Jung, H.Y.; Lee, T.G.; Kang, L.W.; Ahn, Y.J.; Cho, H.S.; Heo, Y.S.
Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK
Biochem. Biophys. Res. Commun.
391
187-192
2010
Homo sapiens (O00763), Homo sapiens
brenda
Monnot, S.; Serre, V.; Chadefaux-Vekemans, B.; Aupetit, J.; Romano, S.; De Lonlay, P.; Rival, J.M.; Munnich, A.; Steffann, J.; Bonnefont, J.P.
Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency
Hum. Mutat.
30
734-740
2009
Homo sapiens
brenda
Chou, C.Y.; Yu, L.P.; Tong, L.
Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism
J. Biol. Chem.
284
11690-11697
2009
Escherichia coli (P24182), Escherichia coli
brenda
Miller, J.R.; Dunham, S.; Mochalkin, I.; Banotai, C.; Bowman, M.; Buist, S.; Dunkle, B.; Hanna, D.; Harwood, H.J.; Huband, M.D.; Karnovsky, A.; Kuhn, M.; Limberakis, C.; Liu, J.Y.; Mehrens, S.; Mueller, W.T.; Narasimhan, L.; Ogden, A.; Ohren, J.; Prasad, J.V.; Shelly, J.A.; Skerlos, L.; Sulavik, M.; Thomas,
A class of selective antibacterials derived from a protein kinase inhibitor pharmacophore
Proc. Natl. Acad. Sci. USA
106
1737-1742
2009
Escherichia coli (P24182)
brenda
Bordelon, T.; Nilsson Lill, S.; Waldrop, G.
The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase
Proteins Struct. Funct. Bioinform.
74
808-819
2009
Escherichia coli
brenda
Yu, L.P.; Xiang, S.; Lasso, G.; Gil, D.; Valle, M.; Tong, L.
A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A
Structure
17
823-832
2009
Staphylococcus aureus (A0A0H3JUV1), Staphylococcus aureus
brenda
Gu, K.; Chiam, H.; Tian, D.; Yin, Z.
Molecular cloning and expression of heteromeric ACCase subunit genes from Jatropha curcas
Plant Sci.
180
642-649
2011
Jatropha curcas (F2WMV4), Jatropha curcas
brenda
Peters-Wendisch, P.; Stansen, K.C.; Goetker, S.; Wendisch, V.F.
Biotin protein ligase from Corynebacterium glutamicum: role for growth and L: -lysine production
Appl. Microbiol. Biotechnol.
93
2493-2502
2012
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
brenda
Dimou, M.; Zografou, C.; Venieraki, A.; Katinakis, P.
Functional interaction of Azotobacter vinelandii cytoplasmic cyclophilin with the biotin carboxylase subunit of acetyl-CoA carboxylase
Biochem. Biophys. Res. Commun.
424
736-739
2012
Azotobacter vinelandii (C1DLJ7), Azotobacter vinelandii
brenda
Sarosiek, N.; Sarzynska, J.; Podkowinski, J.
Modeling of biotin carboxylase from plants
Biotechnologia
94
96-97
2013
Medicago truncatula
-
brenda
Tong, L.
Structure and function of biotin-dependent carboxylases
Cell. Mol. Life Sci.
70
863-891
2013
Escherichia coli
brenda
Smith, A.C.; Cronan, J.E.
Dimerization of the bacterial biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo
J. Bacteriol.
194
72-78
2012
Escherichia coli
brenda
Chou, C.Y.; Tong, L.
Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization
J. Biol. Chem.
286
24417-24425
2011
Escherichia coli (P24182), Escherichia coli
brenda
Novak, B.; Moldovan, D.; Waldrop, G.; De Queiroz, M.
Behavior of the ATP grasp domain of biotin carboxylase monomers and dimers studied using molecular dynamics simulations
Proteins
79
622-632
2011
Escherichia coli
brenda
Broussard, T.C.; Kobe, M.J.; Pakhomova, S.; Neau, D.B.; Price, A.E.; Champion, T.S.; Waldrop, G.L.
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase
Structure
21
650-657
2013
Escherichia coli (P24182), Escherichia coli
brenda
Broussard, T.C.; Pakhomova, S.; Neau, D.B.; Bonnot, R.; Waldrop, G.L.
Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase
Biochemistry
54
3860-3870
2015
Haemophilus influenzae (P43873), Haemophilus influenzae, Haemophilus influenzae DSM 11121 (P43873)
brenda
Brylinski, M.; Waldrop, G.L.
Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries
Molecules
19
4021-4045
2014
Escherichia coli, Haemophilus influenzae, Staphylococcus aureus
brenda