Insight into the Carboxyl Transferase Domain Mechanism of Pyruvate Carboxylase from \u3cem\u3eRhizobium etli\u3c/em\u3e [PDF]
, 2009 The effects of mutations in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase have been determined for the forward reaction to form oxaloacetate, the reverse reaction to form MgATP, the oxamate-induced ...
Attwood, Paul V +5 more
core +1 more source
Crystal structures of trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes [PDF]
, 2013 Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target.
Canning, Peter +3 more
core +3 more sources
Kinetic Analysis of the Catalytic Domain of Human Cdc25B [PDF]
Journal of Biological Chemistry, 1996 The Cdc25 cell cycle regulator is a member of the dual-specificity class of protein-tyrosine phosphatases that hydrolyze phosphotyrosine- and phosphothreonine-containing substrates. To study the mechanism of Cdc25B, we have overexpressed and purified the catalytic domain of human Cdc25B (Xu, X., and Burke, S. P. (1996) J. Biol. Chem.
E B, Gottlin +6 more
openaire +2 more sources
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
FEBS Letters, EarlyView.Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
p97 Disease Mutations Modulate Nucleotide-Induced Conformation to Alter Protein-Protein Interactions. [PDF]
, 2016 The AAA+ ATPase p97/VCP adopts at least three conformations that depend on the binding of ADP and ATP and alter the orientation of the N-terminal protein-protein interaction (PPI) domain into up and down conformations.
Arkin, Michelle +2 more
core
Resuscitation-promoting factors possess a lysozyme-like domain [PDF]
, 2004 The novel bacterial cytokine family – resuscitation-promoting factors (Rpfs) – share a conserved domain of uncharacterized function. Predicting the structure of this domain suggests that Rpfs possess a lysozyme-like domain.
Cohen Gonsaud, M. +5 more
core +1 more source
Journal of Lipid Research, 2018 Delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for PUFA biosynthesis. In some organisms, FADS2s have high substrate specificity, whereas in others, they have high catalytic activity. Previously, we analyzed the molecular mechanisms
Haisu Shi +7 more
doaj +1 more source
Sonic Hedgehog Is a Member of the Hh/DD-Peptidase Family That Spans the Eukaryotic and Bacterial Domains of Life. [PDF]
, 2018 Sonic Hedgehog (Shh) coordinates Zn2+ in a manner that resembles that of peptidases. The ability of Shh to undergo autoproteolytic processing is impaired in mutants that affect the Zn2+ coordination, while mutating residues essential for catalytic ...
Roelink, Henk
core +3 more sources
A Monoclonal Antibody Against the Catalytic Domain of PTP1B [PDF]
Hybridoma, 2012 Protein tyrosine phosphatase 1B (PTP1B), a member of the protein tyrosine phosphatase (PTP) family, plays a crucial role in metabolic signaling, with insulin and leptin signaling being well studied. New evidence indicates that PTP1B is also involved in cancer.
Zeng, Fanwei +9 more
openaire +3 more sources
Structural Evidence of a Major Conformational Change Triggered by Substrate Binding in DapE Enzymes: Impact on the Catalytic Mechanism [PDF]
, 2018 The X-ray crystal structure of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae (HiDapE) bound by the products of hydrolysis, succinic acid and l,l-DAP, was determined at 1.95 Å.
Becker, Daniel P. +9 more
core +1 more source