Panoramic view of a superfamily of phosphatases through substrate profiling

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 16, 2015, Pages E1974-E1983

  Huang, Hua ^a   Pandya, Chetanya ^b,c   Liu, Chunliang ^a   Al Obaidi, Nawar F ^d   Wang, Min ^a   Zheng, Li ^a   Keating, Sarah Toews ^a   Aono, Miyuki ^b   Love, James D ^d   Evans, Brandon ^d   Seidel, Ronald D ^d   Hillerich, Brandan S ^d   Garforth, Scott J ^d   Almo, Steven C ^d   Mariano, Patrick S ^a   Dunaway Mariano, Debra ^a   Allen, Karen N ^b   Farelli, Jeremiah D ^b  

^a UNIVERSITY OF NEW MEXICO   (United States)

^b USA   (United States)

^c BOSTON UNIVERSITY   (United States)

^d ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Evolution; Phosphatase; Promiscuity; Specificity; Substrate screen

Indexed keywords

HALOALKANOATE DEHALOGENASE SUPERFAMILY; PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; ORTHOLOGY; PRIORITY JOURNAL; SCREENING; STEADY STATE; ENZYME SPECIFICITY; HIGH THROUGHPUT SCREENING; KINETICS; METABOLISM; MULTIGENE FAMILY; REPRODUCIBILITY;

PROKARYOTA;

HIGH-THROUGHPUT SCREENING ASSAYS; KINETICS; MULTIGENE FAMILY; PHOSPHORIC MONOESTER HYDROLASES; REPRODUCIBILITY OF RESULTS; SUBSTRATE SPECIFICITY;

EID: 84928253931     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1423570112     Document Type: Article

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