Multiple conformational changes in enzyme catalysis
GG Hammes - Biochemistry, 2002 - ACS Publications
Understanding the molecular mechanisms of enzyme catalysis and allosteric regulation has
been a primary goal of biochemistry for many years. The dynamics of these processes …
been a primary goal of biochemistry for many years. The dynamics of these processes …
Flexibility, diversity, and cooperativity: pillars of enzyme catalysis
This brief review discusses our current understanding of the molecular basis of enzyme
catalysis. A historical development is presented, beginning with steady state kinetics and …
catalysis. A historical development is presented, beginning with steady state kinetics and …
[HTML][HTML] Ornithine aminotransferase, an important glutamate-metabolizing enzyme at the crossroads of multiple metabolic pathways
Ornithine δ-aminotransferase (OAT, EC 2.6. 1.13) catalyzes the transfer of the δ-amino
group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and …
group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and …
PLP-dependent H2S biogenesis
S Singh, R Banerjee - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2011 - Elsevier
The role of endogenously produced H2S in mediating varied physiological effects in
mammals has spurred enormous recent interest in understanding its biology and in …
mammals has spurred enormous recent interest in understanding its biology and in …
Aspartate aminotransferase: an old dog teaches new tricks
MD Toney - Archives of biochemistry and biophysics, 2014 - Elsevier
Aspartate aminotransferase (AAT) is a prototypical pyridoxal 5′-phosphate (PLP)
dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α …
dependent enzyme that catalyzes the reversible interconversion of l-aspartate and α …
[HTML][HTML] Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases
AD Kern, MA Oliveira, P Coffino, ML Hackert - Structure, 1999 - cell.com
Abstract Background: Pyridoxal-5′-phosphate (PLP) dependent enzymes catalyze a broad
range of reactions, resulting in bond cleavage at Cα, Cβ, or Cγ carbons of D and L amino …
range of reactions, resulting in bond cleavage at Cα, Cβ, or Cγ carbons of D and L amino …
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity
S Sugio, GA Petsko, JM Manning, K Soda, D Ringe - Biochemistry, 1995 - ACS Publications
Revised Manuscript Received May 18, 1995® abstract: The three-dimensional structure of D-
amino acid aminotransferase (d-AAT) in the pyridoxamine phosphate form has …
amino acid aminotransferase (d-AAT) in the pyridoxamine phosphate form has …
Dual substrate recognition of aminotransferases
K Hirotsu, M Goto, A Okamoto… - The Chemical Record, 2005 - Wiley Online Library
Abstract Pyridoxal 5′‐phosphate‐dependent aminotransferases reversibly catalyzes the
transamination reaction in which the α‐amino group of amino acid 1 is transferred to the 2 …
transamination reaction in which the α‐amino group of amino acid 1 is transferred to the 2 …
Crystal Structure of the Pyridoxal-5′-phosphate Dependent Cystathionine β-lyase fromEscherichia coliat 1.83 Å
T Clausen, R Huber, B Laber, HD Pohlenz… - Journal of molecular …, 1996 - Elsevier
Cystathionine β-lyase (CBL) is a member of the γ-family of PLP-dependent enzymes, that
cleaves Cβ-S bonds of a broad variety of substrates. The crystal structure of CBL fromE …
cleaves Cβ-S bonds of a broad variety of substrates. The crystal structure of CBL fromE …
NMR studies of solvent-assisted proton transfer in a biologically relevant Schiff base: Toward a distinction of geometric and equilibrium H-bond isotope effects
The tautomeric equilibrium in a Schiff base, N-(3, 5-dibromosalicylidene)-methylamine 1, a
model for the hydrogen bonded structure of the cofactor pyridoxal-5 '-phosphate PLP which …
model for the hydrogen bonded structure of the cofactor pyridoxal-5 '-phosphate PLP which …