Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Abdussalam Adina-Zada"'
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83461 (2013)
The specific targeting of protein to organelles is achieved by targeting signals being recognised by their cognate receptors. Cytosolic chaperones, bound to precursor proteins, are recognized by specific receptors of the import machinery enabling tra
Externí odkaz:
https://doaj.org/article/cd6eb0feb53d4823abe64bd9d4244f7a
Autor:
Abdussalam Adina-Zada, Sarawut Jitrapakdee, John C. Wallace, Paul V. Attwood, Chaiyos Sirithanakorn
Publikováno v:
Biochemistry
l-Aspartate is a regulatory feedback inhibitor of the biotin-dependent enzyme pyruvate carboxylase in response to increased levels of tricarboxylic acid cycle intermediates. Detailed studies of l-aspartate inhibition of pyruvate carboxylase have been
Autor:
Chutima Sereeruk, Tonya N. Zeczycki, W. Wallace Cleland, Martin St. Maurice, Sarawut Jitrapakdee, Abdussalam Adina-Zada, John C. Wallace, Paul V. Attwood
Publikováno v:
Biochemistry. 51:8208-8217
Mutation of Arg427 and Arg472 in Rhizobium etli pyruvate carboxylase to serine or lysine greatly increased the activation constant (K(a)) of acetyl CoA, with the increase being greater for the Arg472 mutants. These results indicate that while both th
Publikováno v:
Archives of Biochemistry and Biophysics. 519:118-130
In this review we examine the effects of the allosteric activator, acetyl CoA on both the structure and catalytic activities of pyruvate carboxylase. We describe how the binding of acetyl CoA produces gross changes to the quaternary and tertiary stru
Autor:
John C. Wallace, Kathy H. Surinya, Paul V. Attwood, Tonya N. Zeczycki, Abdussalam Adina-Zada, Sarawut Jitrapakdee, Martin St. Maurice, Ann L. Menefee, W. Wallace Cleland
Publikováno v:
Biochemistry. 50:9724-9737
The catalytic mechanism of the MgATP-dependent carboxylation of biotin in the biotin carboxylase domain of pyruvate carboxylase from R. etli (RePC) is common to the biotin-dependent carboxylases. The current site-directed mutagenesis study has clarif
Autor:
Paul V. Attwood, Klaus Bergander, Josef Krieglstein, Katrin Ludwig, Paul G. Besant, Susanne Klumpp, Abdussalam Adina-Zada
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:199-205
Using peptides based on the amino acid sequences surrounding the two histidine residues in histone H4, we have investigated the kinetics of the phosphorylation and dephosphorylation reactions of their histidine residues, when reacted with potassium p
Autor:
Abdussalam Adina-Zada, Steven W. Polyak, W. Wallace Cleland, Grant W. Booker, Katharina H. Surinya, Sarawut Jitrapakdee, Cvetan Stojkoski, Paul V. Attwood, Roger Smyth, John C. Wallace
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 39:2120-2134
The native form of pyruvate carboxylase is an alpha4 tetramer but the tetramerisation domain of each subunit is currently unknown. To identify this domain we co-expressed yeast pyruvate carboxylase 1 isozyme (Pyc1) with an N-terminal myc tag, togethe
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 12, p e83461 (2013)
PLoS ONE, Vol 8, Iss 12, p e83461 (2013)
The specific targeting of protein to organelles is achieved by targeting signals being recognised by their cognate receptors. Cytosolic chaperones, bound to precursor proteins, are recognized by specific receptors of the import machinery enabling tra
Autor:
W. Wallace Cleland, Abdussalam Adina-Zada, Rasmani Hazra, Sarawut Jitrapakdee, Chutima Sereeruk, Tonya N. Zeczycki, Paul V. Attwood, Martin St. Maurice, John C. Wallace
Publikováno v:
Archives of biochemistry and biophysics. 509(2)
2′,3′-O-(2,4,6-Trinitrophenyl) adenosine 5′-triphosphate (TNP-ATP) is a fluorescent analogue of ATP. MgTNP-ATP was found to be an allosteric activator of pyruvate carboxylase that exhibits competition with acetyl CoA in activating the enzyme. T
Autor:
Saowapa Duangpan, Sarawut Jitrapakdee, W. Wallace Cleland, Lindsay T. Byrne, Martin St. Maurice, Paul V. Attwood, John C. Wallace, Tonya N. Zeczycki, Abdussalam Adina-Zada
Pyruvate carboxylase (PC) (EC 6.4.1.1), a biotin-containing enzyme, catalyses pyruvate carboxylation through a two-step reaction shown in Figure 1 (1, 2). In reaction [1] (Fig. 1), the carboxylation of biotin in the biotin carboxylase (BC) domain is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccb75896ad84c57bc1a7f6ecb036a8f6
https://europepmc.org/articles/PMC2864305/
https://europepmc.org/articles/PMC2864305/