scholarly journals Uncovering divergent evolution of α/β-hydrolases: a surprising residue substitution needed to convert Hevea brasiliensis hydroxynitrile lyase into an esterase

2014 ◽  
Vol 5 (11) ◽  
pp. 4265-4277 ◽  
Author(s):  
David M. Nedrud ◽  
Hui Lin ◽  
Gilsinia Lopez ◽  
Santosh K. Padhi ◽  
Graig A. Legatt ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Active Site ◽  
Hevea Brasiliensis ◽  
Divergent Evolution ◽  
Hydroxynitrile Lyase ◽  
Residue Substitution ◽  
Active Site Histidine

Although Glu79 does not contribute to esterase catalysis, it can block esterase catalysis by hydrogen bonding to the active site histidine.

Identification of an active site histidine in urokinase

1976 ◽  
Vol 429 (1) ◽  
pp. 252-257 ◽  
Author(s):  
Eng Bee Ong ◽  
Alan J. Johnson ◽  
Guenther Schoellmann
Keyword(s):  
Active Site ◽  
Active Site Histidine

scholarly journals About the pKaof the active-site histidine in flavocytochrome b2(yeast L-lactate dehydrogenase)

1998 ◽  
Vol 7 (7) ◽  
pp. 1531-1537 ◽  
Author(s):  
K. Sudhindra Rao ◽  
Florence Lederer
Keyword(s):  
Lactate Dehydrogenase ◽  
Active Site ◽  
Flavocytochrome B2 ◽  
Active Site Histidine

scholarly journals How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Dariusz Czernecki ◽  
Pierre Legrand ◽  
Mustafa Tekpinar ◽  
Sandrine Rosario ◽  
Pierre-Alexandre Kaminski ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonding ◽  
Crystal Structures ◽  
Active Site ◽  
Metal Ion ◽  
Restriction Endonucleases ◽  
Structural Element

AbstractBacteriophages have long been known to use modified bases in their DNA to prevent cleavage by the host’s restriction endonucleases. Among them, cyanophage S-2L is unique because its genome has all its adenines (A) systematically replaced by 2-aminoadenines (Z). Here, we identify a member of the PrimPol family as the sole possible polymerase of S-2L and we find it can incorporate both A and Z in front of a T. Its crystal structure at 1.5 Å resolution confirms that there is no structural element in the active site that could lead to the rejection of A in front of T. To resolve this contradiction, we show that a nearby gene is a triphosphohydolase specific of dATP (DatZ), that leaves intact all other dNTPs, including dZTP. This explains the absence of A in S-2L genome. Crystal structures of DatZ with various ligands, including one at sub-angstrom resolution, allow to describe its mechanism as a typical two-metal-ion mechanism and to set the stage for its engineering.

scholarly journals Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the ‘RED’ family)

1994 ◽  
Vol 304 (1) ◽  
pp. 95-99 ◽  
Author(s):  
G Labesse ◽  
A Vidal-Cros ◽  
J Chomilier ◽  
M Gaudry ◽  
J P Mornon
Keyword(s):  
Amino Acids ◽  
Sequence Alignment ◽  
Active Site ◽  
Tertiary Structure ◽  
Binding Specificity ◽  
Single Domain ◽  
Divergent Evolution ◽  
Cofactor Binding ◽  
Sequence Identity ◽  
Definition Of

Using both primary- and tertiary-structure comparisons, we have established new structural similarities shared by reductases, epimerases and dehydrogenases not previously known to be related. Despite the low sequence identity (down to 10%), short consensus segments are identified. We show that the sequence, the active site and the supersecondary structure are well conserved in these proteins. New homologues (the protochlorophyllide reductases) are detected, and we define a new superfamily composed of single-domain dinucleotide-binding enzymes. Rules for the cofactor-binding specificity are deduced from our sequence alignment. The involvement of some amino acids in catalysis is discussed. Comparison with two-domain dehydrogenases allows us to distinguish two general mechanisms of divergent evolution.

scholarly journals Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis

2002 ◽  
Vol 269 (3) ◽  
pp. 893-901 ◽  
Author(s):  
Evert Bokma ◽  
Henriëtte J. Rozeboom ◽  
Mark Sibbald ◽  
Bauke W. Dijkstra ◽  
Jaap J. Beintema
Keyword(s):  
Active Site ◽  
Hevea Brasiliensis ◽  
Rubber Tree ◽  
Active Site Mutants
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