> top > docs > PubMed:13679361 > annotations

PubMed:13679361 JSONTXT

Annnotations TAB JSON ListView MergeView

sentences

Id Subject Object Predicate Lexical cue
T1 0-92 Sentence denotes Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi).
T2 93-293 Sentence denotes Ribose-5-phosphate isomerase (Rpi) acts as a key enzyme in the oxidative and reductive pentose-phosphate pathways for the conversion of ribose-5-phosphate (R5P) to ribulose-5-phosphate and vice versa.
T3 294-548 Sentence denotes We have determined the crystal structures of Rpi from Thermus thermophilus HB8 in complex with the open chain form of the substrate R5P and the open chain form of the C2 epimeric inhibitor arabinose-5-phosphate as well as the apo form at high resolution.
T4 549-693 Sentence denotes The crystal structures of both complexes revealed that these ring-opened epimers are bound in the active site in a mirror symmetry binding mode.
T5 694-806 Sentence denotes The O1 atoms are stabilized by an oxyanion hole composed of the backbone amide nitrogens in the conserved motif.
T6 807-982 Sentence denotes In the structure of the Rpi.R5P complex, the conversion moiety O1-C1-C2-O2 in cis-configuration interacts with the carboxyl oxygens of Glu-108 in a water-excluded environment.
T7 983-1109 Sentence denotes Furthermore, the C2 hydroxyl group is presumed to be highly polarized by short hydrogen bonding with the side chain of Lys-99.
T8 1110-1321 Sentence denotes R5P bound as the ring-opened reaction intermediate clarified the high stereoselectivity of the catalysis and is consistent with an aldose-ketose conversion by Rpi that proceeds via a cis-enediolate intermediate.

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 348-368 OrganismTaxon denotes Thermus thermophilus 274

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 758-766 Body_part denotes backbone http://purl.obolibrary.org/obo/UBERON_0001130