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1 is communication between the two subunits of biotin carboxylase.
2 tuted with purified, recombinant Arabidopsis biotin carboxylase.
3  to several different reactions catalyzed by biotin carboxylase.
4 the substrate-induced synergism by biotin in biotin carboxylase.
5 c component are similar to those observed in biotin carboxylase.
6 etermined for D-alanine:D-alanine ligase and biotin carboxylase.
7 richia coli form of the enzyme consists of a biotin carboxylase activity, a biotin carboxyl carrier p
8                   In comparison to wild-type biotin carboxylase, all four mutant enzymes gave very si
9 its: biotin carboxyl-carrier protein (BCCP), biotin carboxylase, alpha-carboxyltransferase, and beta-
10  the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles.
11 ce identities (33-62%) to, respectively, the biotin carboxylase and biotin carboxyl carrier + carboxy
12 B- and C-domains, and in some cases, such as biotin carboxylase and carbamoyl phosphate synthetase, t
13 dine 1 and moiramide B (3) which bind to the biotin carboxylase and carboxyltransferase ACC active si
14 otein (holoBCCP87) to act as a substrate for biotin carboxylase and carboxyltransferase was assessed
15  acid synthesis and consists of two enzymes: biotin carboxylase and carboxyltransferase.
16  the X-ray crystal structure coordinates for biotin carboxylase and D-alanine:D-alanine ligase.
17 res of two mechanistically related proteins, biotin carboxylase and D-alanine:D-alanine ligase.
18  alpha-keto acid dehydrogenase E1 component, biotin carboxylase and superoxide dismutase were related
19 lear-coded subunits (biotin carboxy-carrier, biotin carboxylase, and alpha-carboxyltransferase).
20 yn is similar to D-alanine:D-alanine ligase, biotin carboxylase, and glutathione synthetase, despite
21  in vivo data indicate that both subunits of biotin carboxylase are required for activity and that th
22 r, structural data are available for E. coli biotin carboxylase as is a system for its overexpression
23 f the residues in the catalytic mechanism of biotin carboxylase as well as to establish a molecular b
24               The alpha-subunit contains the biotin carboxylase (BC) and biotin carboxyl carrier prot
25           Hints of a sub-complex between the biotin carboxylase (BC) and biotin carboxyl carrier prot
26 ylase (LmPC), a biotin-dependent enzyme with biotin carboxylase (BC) and carboxyltransferase (CT) act
27                                 ACC contains biotin carboxylase (BC) and carboxyltransferase (CT) act
28 ctions catalyzed by the holo-ACC components, biotin carboxylase (BC) and carboxyltransferase (CT), we
29  they can competently and independently bind biotin carboxylase (BC) but differ in responses to pH ch
30 al potency of pyridopyrimidine inhibitors of biotin carboxylase (BC) by up to 64-fold and 16-fold aga
31              These enzymes share a conserved biotin carboxylase (BC) component, which catalyzes the A
32 roduct, is a nanomolar inhibitor against the biotin carboxylase (BC) domain of human, yeast, and othe
33                                              Biotin carboxylase (BC) is a conserved component among b
34                                          The biotin carboxylase (BC) subunit of Escherichia coli ACC
35 omponents that constitute plastid ACCase are biotin carboxylase (BC), biotin carboxyl carrier protein
36                                          The biotin carboxylase (BC), biotin carboxyl carrier protein
37 1.2) is a multisubunit complex consisting of biotin carboxylase (BC), biotin-carboxyl carrier protien
38                                  PC contains biotin carboxylase (BC), carboxyltransferase (CT) and bi
39  enzyme consists of four catalytic subunits: biotin carboxylase (BC), carboxyltransferase (CT)-alpha,
40 first enzymatic activity of the ACC complex, biotin carboxylase (BC), catalyzes the carboxylation of
41 t least four different protein subunits: the biotin carboxylase (BC), the biotin carboxyl carrier pro
42 dopyrimidines target the ATP-binding site of biotin carboxylase (BC), which catalyzes the first enzym
43 mposed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and
44 a coli acetyl-CoA carboxylase is composed of biotin carboxylase, carboxyltransferase and biotin carbo
45 nzyme consisting of three separate proteins: biotin carboxylase, carboxyltransferase, and the biotin
46 g of three distinct and separate components: biotin carboxylase, carboxyltransferase, and the biotin
47 id (pTrc.BCCP) encodes the C terminus of the biotin carboxylase carrier protein (BCCP) under the cont
48  in 1.3S contrasts with the findings for the biotin carboxylase carrier protein from E. coli acetyl-C
49                                              Biotin carboxylase catalyzes the ATP-dependent carboxyla
50                                              Biotin carboxylase catalyzes the ATP-dependent carboxyla
51 e three-dimensional structure of the E. coli biotin carboxylase complexed with ATP and determined to
52                                          The biotin carboxylase component catalyzes the ATP-dependent
53                                          The biotin carboxylase component catalyzes the ATP-dependent
54                                          The biotin carboxylase component has served for many years a
55  system for site-directed mutagenesis of the biotin carboxylase component is described.
56                                          The biotin carboxylase component, which catalyzes the ATP-de
57               Using the crystal structure of biotin carboxylase, cysteine 230 and lysine 238 were ide
58           The three-dimensional structure of biotin carboxylase, determined by x-ray crystallography,
59                  In vitro kinetic studies of biotin carboxylase dimers in which both subunits were wi
60 osthetic group must first gain access to the biotin carboxylase domain and become carboxylated and th
61 mmetrical conformation in the absence of the biotin carboxylase domain and that the carboxyltransfera
62               The amino acid sequence of the biotin carboxylase domain encoded by Acc-1,1 and Acc-1,2
63              Fragments of genes encoding the biotin carboxylase domain of multidomain ACCs of T. gond
64 pyruvate and oxamate on the reactions of the biotin carboxylase domain.
65                         In Escherichia coli, biotin carboxylase exists as a homodimer where each subu
66                                              Biotin carboxylase from Escherichia coli catalyzes the A
67                     Expression of the mutant biotin carboxylase genes from an inducible arabinose pro
68                               In the case of biotin carboxylase holoBCCP87 was an excellent substrate
69  The catalytic properties of the recombinant biotin carboxylase indicate that the activity of the het
70                         The Escherichia coli biotin carboxylase is readily isolated from the other co
71                     Numerical simulations of biotin carboxylase kinetics were the most similar to the
72                    Four of these residues of biotin carboxylase, Lys-116, Lys-159, His-209, and Glu-2
73      However, kinetic assays of hybrid dimer biotin carboxylase molecules in which one subunit had an
74  whether novel ACCase inhibitors inhibit the biotin carboxylase or carboxyltransferase site of ACCase
75 richia coli form of the enzyme consists of a biotin carboxylase protein, a biotin carboxyl carrier pr
76 volved in abiotic stress response, including biotin carboxylase, serine/threonine-protein kinase, and
77                                          The biotin carboxylase subunit of the heteromeric chloroplas
78            Holo-BCCP then interacts with the biotin carboxylase subunit, which leads to the addition
79    The M. tuberculosis genome contains three biotin carboxylase subunits (AccA1 to -3) and six carbox
80 tide probe representing conserved regions of biotin carboxylase subunits of acetyl coenzyme A (acetyl
81 d by the accA gene was strikingly similar to biotin carboxylase subunits of acetyl-CoA and propionyl-
82 se, which has an analogous mode of action to biotin carboxylase, suggests the catalytic base in this
83 e constructed three site-directed mutants of biotin carboxylase that are homologous to three missense
84 cherichia coli and the resulting recombinant biotin carboxylase was enzymatically active in carboxyla
85 y structure of an unliganded form of E. coli biotin carboxylase was originally solved in 1994 to 2.4-
86 bunit contributes to the overall function of biotin carboxylase, we made hybrid molecules in which on
87 ype, hybrid dimers, and mutant homodimers of biotin carboxylase were performed.
88 e mutants M169K, R338Q, and R338S of E. coli biotin carboxylase were selected for study to mimic the
89 y of the ATP synthesis reaction catalyzed by biotin carboxylase where carbamoyl phosphate reacts with
90 Stimulation of the ATP synthesis reaction of biotin carboxylase where carbamyl phosphate reacted with
91          A comparison of this closed form of biotin carboxylase with carbamoyl-phosphate synthetase i
92           The V/K or catalytic efficiency of biotin carboxylase with holoBCCP87 as substrate was 8000