scholarly journals Characterizing the Importance of the Biotin Carboxylase Domain Dimer for Staphylococcus aureus Pyruvate Carboxylase Catalysis

Biochemistry ◽  
2013 ◽  
Vol 52 (3) ◽  
pp. 488-496 ◽  
Author(s):  
Linda P. C. Yu ◽  
Chi-Yuan Chou ◽  
Philip H. Choi ◽  
Liang Tong
Keyword(s):  
Staphylococcus Aureus ◽  
Pyruvate Carboxylase ◽  
Biotin Carboxylase

Kinetic and Thermodynamic Analysis of Acetyl-CoA Activation of Staphylococcus aureus Pyruvate Carboxylase

Biochemistry ◽  
2017 ◽  
Vol 56 (27) ◽  
pp. 3492-3506 ◽  
Author(s):  
Lauren E. Westerhold ◽  
Lance C. Bridges ◽  
Saame Raza Shaikh ◽  
Tonya N. Zeczycki
Keyword(s):  
Staphylococcus Aureus ◽  
Thermodynamic Analysis ◽  
Pyruvate Carboxylase ◽  
Acetyl Coa ◽  
Kinetic And Thermodynamic Analysis

scholarly journals Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase fromRhizobium etli

Biochemistry ◽  
2011 ◽  
Vol 50 (45) ◽  
pp. 9708-9723 ◽  
Author(s):  
Adam D. Lietzan ◽  
Ann L. Menefee ◽  
Tonya N. Zeczycki ◽  
Sudhanshu Kumar ◽  
Paul V. Attwood ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Biotin Carboxylase

Structure of the biotin carboxylase domain of pyruvate carboxylase fromBacillus thermodenitrificans

2007 ◽  
Vol 63 (8) ◽  
pp. 885-890 ◽  
Author(s):  
Shin Kondo ◽  
Yoshitaka Nakajima ◽  
Shigetoshi Sugio ◽  
Shinji Sueda ◽  
Md Nurul Islam ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Biotin Carboxylase

scholarly journals Novel Insights into the Biotin Carboxylase Domain Reactions of Pyruvate Carboxylase fromRhizobium etli

Biochemistry ◽  
2011 ◽  
Vol 50 (45) ◽  
pp. 9724-9737 ◽  
Author(s):  
Tonya N. Zeczycki ◽  
Ann L. Menefee ◽  
Abdussalam Adina-Zada ◽  
Sarawut Jitrapakdee ◽  
Kathy H. Surinya ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Biotin Carboxylase

scholarly journals Structure, mechanism and regulation of pyruvate carboxylase

2008 ◽  
Vol 413 (3) ◽  
pp. 369-387 ◽  
Author(s):  
Sarawut Jitrapakdee ◽  
Martin St Maurice ◽  
Ivan Rayment ◽  
W. Wallace Cleland ◽  
John C. Wallace ◽  
...  
Keyword(s):  
Active Site ◽  
Pyruvate Carboxylase ◽  
Polypeptide Chain ◽  
Tricarboxylic Acid Cycle ◽  
Biotin Carboxylase ◽  
Acetyl Coa ◽  
Specific Expression ◽  
Allosteric Effector ◽  
Bona Fide ◽  
And Function

PC (pyruvate carboxylase) is a biotin-containing enzyme that catalyses the HCO3−- and MgATP-dependent carboxylation of pyruvate to form oxaloacetate. This is a very important anaplerotic reaction, replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways. PC is therefore considered as an enzyme that is crucial for intermediary metabolism, controlling fuel partitioning toward gluconeogenesis or lipogenesis and in insulin secretion. The enzyme was discovered in 1959 and over the last decade there has been much progress in understanding its structure and function. PC from most organisms is a tetrameric protein that is allosterically regulated by acetyl-CoA and aspartate. High-resolution crystal structures of the holoenzyme with various ligands bound have recently been determined, and have revealed details of the binding sites and the relative positions of the biotin carboxylase, carboxyltransferase and biotin carboxyl carrier domains, and also a unique allosteric effector domain. In the presence of the allosteric effector, acetyl-CoA, the biotin moiety transfers the carboxy group between the biotin carboxylase domain active site on one polypeptide chain and the carboxyltransferase active site on the adjacent antiparallel polypeptide chain. In addition, the bona fide role of PC in the non-gluconeogenic tissues has been studied using a combination of classical biochemistry and genetic approaches. The first cloning of the promoter of the PC gene in mammals and subsequent transcriptional studies reveal some key cognate transcription factors regulating tissue-specific expression. The present review summarizes these advances and also offers some prospects in terms of future directions for the study of this important enzyme.

Structure of the biotin carboxylase subunit of pyruvate carboxylase fromAquifex aeolicusat 2.2 Å resolution

2004 ◽  
Vol 60 (3) ◽  
pp. 486-492 ◽  
Author(s):  
Shin Kondo ◽  
Yoshitaka Nakajima ◽  
Shigetoshi Sugio ◽  
Jin Yong-Biao ◽  
Shinji Sueda ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Biotin Carboxylase

Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers

2007 ◽  
Vol 39 (11) ◽  
pp. 2120-2134 ◽  
Author(s):  
Sarawut Jitrapakdee ◽  
Katharina H. Surinya ◽  
Abdussalam Adina-Zada ◽  
Steven W. Polyak ◽  
Cvetan Stojkoski ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Biotin Carboxylase
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