Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity

Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity

Item
http://www.wikidata.org/entity/Q27637594
Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator)Crystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate RecognitionStructural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosisStructural Units Important for Activity of a Novel-type Phosphoserine Phosphatase from Hydrogenobacter thermophilus TK-6 Revealed by Crystal Structure AnalysisStructural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutaseMechanism of Dephosphorylation of Glucosyl-3-phosphoglycerate by a Histidine PhosphataseSeeing the process of histidine phosphorylation in human bisphosphoglycerate mutaseCrystal structure of human bisphosphoglycerate mutaseStructural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphataseUnexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase.Functional characterization of two members of histidine phosphatase superfamily in Mycobacterium tuberculosis.Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species.Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.Crystallization and preliminary X-ray diffraction analysis of a novel type of phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6.Cofactor-independent phosphoglycerate mutase has an essential role in Caenorhabditis elegans and is conserved in parasitic nematodes.Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation.Recent developments in MrBUMP: better search-model preparation, graphical interaction with search models, and solution improvement and assessment.
P2860

Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity

Item
http://www.wikidata.org/entity/Q27637594
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
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2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structure and mechanism of act ...... ecificity phosphatase activity
@ast
Structure and mechanism of act ...... ecificity phosphatase activity
@en
Structure and mechanism of act ...... ecificity phosphatase activity
@nl
type
label
Structure and mechanism of act ...... ecificity phosphatase activity
@ast
Structure and mechanism of act ...... ecificity phosphatase activity
@en
Structure and mechanism of act ...... ecificity phosphatase activity
@nl
prefLabel
Structure and mechanism of act ...... ecificity phosphatase activity
@ast
Structure and mechanism of act ...... ecificity phosphatase activity
@en
Structure and mechanism of act ...... ecificity phosphatase activity
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Structure and mechanism of act ...... ecificity phosphatase activity
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698