scholarly journals The crystal structure of AbsH3 : A putative flavin adenine dinucleotide‐dependent reductase in the abyssomicin biosynthesis pathway

2020 ◽  
Vol 89 (1) ◽  
pp. 132-137
Author(s):  
Jonathan A. Clinger ◽  
Xiachang Wang ◽  
Wenlong Cai ◽  
Yanyan Zhu ◽  
Mitchell D. Miller ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Flavin Adenine Dinucleotide ◽  
Biosynthesis Pathway

scholarly journals Threonine 57 is required for the post-translational activation ofEscherichia coliaspartate α-decarboxylase

2014 ◽  
Vol 70 (4) ◽  
pp. 1166-1172 ◽  
Author(s):  
Michael E. Webb ◽  
Briony A. Yorke ◽  
Tom Kershaw ◽  
Sarah Lovelock ◽  
Carina M. C. Lobley ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Intramolecular Rearrangement ◽  
Directed Mutagenesis ◽  
Vitamin B ◽  
Biosynthesis Pathway ◽  
Serine Residue ◽  
Translational Activation

Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formedviathe intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation.

scholarly journals Crystal Structure and Mechanistic Implications of N2-(2-Carboxyethyl)arginine Synthase, the First Enzyme in the Clavulanic Acid Biosynthesis Pathway

2003 ◽  
Vol 279 (7) ◽  
pp. 5685-5692 ◽  
Author(s):  
Matthew E. C. Caines ◽  
Jonathan M. Elkins ◽  
Kirsty S. Hewitson ◽  
Christopher J. Schofield
Keyword(s):  
Crystal Structure ◽  
Clavulanic Acid ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis

scholarly journals Crystal Structure of the Active Site Mutant Form of Soluble Fumarate Reductase, Osm1

Crystals ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 504 ◽  
Author(s):  
Kim ◽  
Kwon ◽  
Jung ◽  
Chun ◽  
Ha ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Flavin Adenine Dinucleotide ◽  
Structural Information ◽  
Redox Balance ◽  
Underlying Mechanism ◽  
Fumarate Reductase ◽  
Mutant Form ◽  
Characteristic Features ◽  
Fad Binding

Soluble fumarate reductase is essential for survival under anaerobic conditions. This enzyme can maintain the redox balance in the cell by catalyzing the reduction of fumarate to succinate. Although the overall reaction mechanism of soluble fumarate reductase in yeast, Osm1, has been proposed by a previous structural study, the details of the underlying mechanism are not completely elucidated. The present study provides the structural information regarding the active site mutant form of Osm1 (R326A), thus, revealing that R326A mutation does not affect the substrate binding. Structural alterations of the residues surrounding the active site, and the missing 2nd flavin adenine dinucleotide (FAD) in the previously defined 2nd FAD binding site, were observed as characteristic features of the Osm1 R326A crystal structure. Based on these findings, we provided a clue that can explain the loss of activity of Osm1 R326A.

scholarly journals Structural Basis for Different Substrate Specificities of Two ADP-Ribose Pyrophosphatases from Thermus thermophilus HB8

2007 ◽  
Vol 190 (3) ◽  
pp. 1108-1117 ◽  
Author(s):  
Taisuke Wakamatsu ◽  
Noriko Nakagawa ◽  
Seiki Kuramitsu ◽  
Ryoji Masui
Keyword(s):  
Crystal Structure ◽  
Flavin Adenine Dinucleotide ◽  
Thermus Thermophilus ◽  
High Specificity ◽  
Ternary Complexes ◽  
Structural Basis ◽  
Water Molecules ◽  
Substrate Specificities ◽  
Catalytic Mechanisms

ABSTRACT ADP-ribose (ADPR) is one of the main substrates of Nudix proteins. Among the eight Nudix proteins of Thermus thermophilus HB8, we previously determined the crystal structure of Ndx4, an ADPR pyrophosphatase (ADPRase). In this study we show that Ndx2 of T. thermophilus also preferentially hydrolyzes ADPR and flavin adenine dinucleotide and have determined its crystal structure. We have determined the structures of Ndx2 alone and in complex with Mg2+, with Mg2+ and AMP, and with Mg2+ and a nonhydrolyzable ADPR analogue. Although Ndx2 recognizes the AMP moiety in a manner similar to those for other ADPRases, it recognizes the terminal ribose in a distinct manner. The residues responsible for the recognition of the substrate in Ndx2 are not conserved among ADPRases. This may reflect the diversity in substrate specificity among ADPRases. Based on these results, we propose the classification of ADPRases into two types: ADPRase-I enzymes, which exhibit high specificity for ADPR; and ADPRase-II enzymes, which exhibit low specificity for ADPR. In the active site of the ternary complexes, three Mg2+ ions are coordinated to the side chains of conserved glutamate residues and water molecules. Substitution of Glu90 and Glu94 with glutamine suggests that these residues are essential for catalysis. These results suggest that ADPRase-I and ADPRase-II enzymes have nearly identical catalytic mechanisms but different mechanisms of substrate recognition.

scholarly journals Crystal structure of thebaine 6-O-demethylase from the morphine biosynthesis pathway

2018 ◽  
Vol 202 (3) ◽  
pp. 229-235 ◽  
Author(s):  
Anna Kluza ◽  
Ewa Niedzialkowska ◽  
Katarzyna Kurpiewska ◽  
Zuzanna Wojdyla ◽  
Matthew Quesne ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Biosynthesis Pathway

scholarly journals Structure of GUN4 fromChlamydomonas reinhardtii

2015 ◽  
Vol 71 (8) ◽  
pp. 1094-1099 ◽  
Author(s):  
Shabnam Tarahi Tabrizi ◽  
David B. Langley ◽  
Stephen J. Harrop ◽  
Anthony P. Duff ◽  
Robert D. Willows
Keyword(s):  
Crystal Structure ◽  
Chlamydomonas Reinhardtii ◽  
Chlorophyll Biosynthesis ◽  
Conformational Dynamics ◽  
Protoporphyrin Ix ◽  
Biosynthesis Pathway ◽  
Broad Agreement ◽  
Binding Cleft ◽  
Mg Chelatase

The genomes uncoupled 4 (GUN4) protein stimulates chlorophyll biosynthesis by increasing the activity of Mg-chelatase, the enzyme that inserts magnesium into protoporphyrin IX (PPIX) in the chlorophyll biosynthesis pathway. One of the roles of GUN4 is in binding PPIX and Mg-PPIX. In eukaryotes, GUN4 also participates in plastid-to-nucleus signalling, although the mechanism for this is unclear. Here, the first crystal structure of a eukaryotic GUN4, fromChlamydomonas reinhardtii, is presented. The structure is in broad agreement with those of previously solved cyanobacterial structures. Most interestingly, conformational divergence is restricted to several loops which cover the porphyrin-binding cleft. The conformational dynamics suggested by this ensemble of structures lend support to the understanding of how GUN4 binds PPIX or Mg-PPIX.

Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases

Biochemistry ◽  
1993 ◽  
Vol 32 (43) ◽  
pp. 11507-11515 ◽  
Author(s):  
Jiayao Li ◽  
Alice Vrielink ◽  
Peter Brick ◽  
David M. Blow
Keyword(s):  
Crystal Structure ◽  
Flavin Adenine Dinucleotide ◽  
Cholesterol Oxidase ◽  
Steroid Substrate

scholarly journals The Crystal Structure of AbsH3: a Putative FAD-dependent Reductase in the Abyssomicin Biosynthesis Pathway.

2020 ◽  
Author(s):  
Jonathan Clinger ◽  
Xiachang Wang ◽  
Wenlong Cai ◽  
Yanyan Zhu ◽  
Mitchell Miller ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Biosynthesis Pathway
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