R
Ricardo Marti-Arbona
Researcher at Los Alamos National Laboratory
Publications - 22
Citations - 507
Ricardo Marti-Arbona is an academic researcher from Los Alamos National Laboratory. The author has contributed to research in topics: Active site & Hydrolase. The author has an hindex of 9, co-authored 20 publications receiving 481 citations. Previous affiliations of Ricardo Marti-Arbona include Texas A&M University & University of California, San Francisco.
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Journal ArticleDOI
Structure-based activity prediction for an enzyme of unknown function
Johannes C. Hermann,Ricardo Marti-Arbona,Alexander A. Fedorov,Elena V. Fedorov,Steven C. Almo,Brian K. Shoichet,Frank M. Raushel +6 more
TL;DR: Structural-based docking with high-energy forms of potential substrates may be a useful tool to annotate enzymes for function.
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High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli.
TL;DR: Structural analysis confirms the placement of isoaspartyl dipeptidase into the urease-related amidohydrolase superfamily and proposes that the reaction mechanism of the enzyme proceeds through a tetrahedral intermediate and that the bridging solvent attacks the re face of the carbonyl carbon of the scissile peptide bond.
Journal ArticleDOI
Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily.
Ricardo Marti-Arbona,Chengfu Xu,Sondra Steele,Amanda Weeks,Gabriel F. Kuty,Clara M. Seibert,Frank M. Raushel +6 more
TL;DR: Three proteins in P. aeruginosa have been identified that catalyze two of the three possible pathways for the degradation of N-formimino-L-glutamate, and the function of Pa5106 has been annotated as a probablechlorohydrolase or cytosine deaminase.
Journal ArticleDOI
Mechanism of the Reaction Catalyzed by Isoaspartyl Dipeptidase from Escherichia coli
Ricardo Marti-Arbona,Vicente Fresquet,James B. Thoden,Melissa L. Davis,Hazel M. Holden,Frank M. Raushel +5 more
TL;DR: The catalytic properties of the wild-type and mutant enzymes, coupled with the X-ray crystal structure of the D285N mutant complexed with beta-Asp-His, are consistent with a chemical reaction mechanism for the hydrolysis of dipeptides that is initiated by the polarization of the amide bond via complexation to the beta-metal ion of the binuclear metal center.
Journal ArticleDOI
The Hunt for 8-Oxoguanine Deaminase
Richard S. Hall,Alexander A. Fedorov,Ricardo Marti-Arbona,Elena V. Fedorov,Peter Kolb,J. Michael Sauder,Stephen K. Burley,Brian K. Shoichet,Steven C. Almo,Frank M. Raushel +9 more
TL;DR: An enzyme from Pseudomonas aeruginosa, Pa0142 (gi|9945972), that is able to catalyze the deamination of 8-oxoguanine (8-oxoG) to uric acid has been identified for the first time.