2015
DOI: 10.1021/acs.biochem.5b00340
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Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase

Abstract: Acetyl-CoA carboxylase catalyzes the first and regulated step in fatty acid synthesis. In most Gram-negative and Gram-positive bacteria, the enzyme is composed of three proteins: biotin carboxylase, a biotin carboxyl carrier protein (BCCP), and carboxyltransferase. The reaction mechanism involves two half-reactions with biotin carboxylase catalyzing the ATP-dependent carboxylation of biotin-BCCP in the first reaction. In the second reaction, carboxyltransferase catalyzes the transfer of the carboxyl group from… Show more

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Cited by 14 publications
(25 citation statements)
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References 48 publications
(119 reference statements)
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“…Carboxybiotin-interacting residues have been identified in the Figure S4. crystal structure of the H. influenzae ACC BC (Broussard et al, 2015) and are structurally conserved in Dra YCC (lysine 235, arginine 290, and arginine 342; Figure 3B), in agreement with a generally conserved BC mechanism.…”
Section: Limited Proteolysis Enables Structure Determination Of Dimersupporting
confidence: 64%
See 1 more Smart Citation
“…Carboxybiotin-interacting residues have been identified in the Figure S4. crystal structure of the H. influenzae ACC BC (Broussard et al, 2015) and are structurally conserved in Dra YCC (lysine 235, arginine 290, and arginine 342; Figure 3B), in agreement with a generally conserved BC mechanism.…”
Section: Limited Proteolysis Enables Structure Determination Of Dimersupporting
confidence: 64%
“…The B subdomain is flexibly tethered by two irregular peptide linkers and exhibits increased disorder in the crystal (Figure S4B). Based on homology to the BC domains of E. coli or Haemophilus influenzae ACC, this B subdomain may undergo a hinge-bending motion during substrate binding to act as a lid to the BC active site (Broussard et al, 2015;Thoden et al, 2000). Particularly the highly conserved glycine-rich loop (lysine 157-methionine 167) in the B subdomain might be involved in direct ligand contacts, with lysine 157 presumably interacting with one of the a-phosphoryl oxygens of MgATP ( Figure 3A).…”
Section: Limited Proteolysis Enables Structure Determination Of Dimermentioning
confidence: 99%
“…3B). The residue in this position interacts directly with the bound nucleotide and is expected to influence the properties of the loop and the residues directly downstream which line the biotin‐binding site, for example, K247, the equivalent residue of K238 in the E. coli protein, shown to influence both the K m for ATP as well as being involved in the carboxylation reaction 12, 47, 48. The substitution to tyrosine is likely to change the properties of both the nucleotide‐binding site and the active site‐bridging loop.…”
Section: Resultsmentioning
confidence: 99%
“…The AccD transcarboxylase enzyme then transfers the CO 2 from carboxybiotin to the CoA ester substrate 6, 12, 13.…”
mentioning
confidence: 99%
“…The conversion of urea begins at its C‐terminal urea carboxylase (UC) domain, processing the carboxylation of urea to generate the intermediate product allophanate, which then presumably diffuses into the N‐terminal allophanate hydrolyse (AH) domain to be further hydrolyzed into ammonium . The UC domain belongs to the biotin‐dependent carboxylase family which share common features of domain organization . They all consist of biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyl transferase (CT) domains, but in different arrangements (Figure a).…”
Section: Introductionmentioning
confidence: 99%