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Structural Determinants of Substrate Recognition in the HAD Superfamily Member d - glycero - d - manno -Heptose-1,7-bisphosphate Phosphatase (GmhB),Divergence of Structure and Function in the Haloacid Dehalogenase Enzyme Superfamily: Bacteroides thetaiotaomicron BT2127 Is an Inorganic PyrophosphataseThe X-ray crystallographic structure and specificity profile of HAD superfamily phosphohydrolase BT1666: Comparison of paralogous functions inB. thetaiotaomicronThe Crystal Structure of Arabidopsis VSP1 Reveals the Plant Class C-Like Phosphatase Structure of the DDDD Superfamily of PhosphohydrolasesDiscovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosisStructural Basis for the Divergence of Substrate Specificity and Biological Function within HAD Phosphatases in Lipopolysaccharide and Sialic Acid BiosynthesisEvolutionary and Structural Analyses of Mammalian Haloacid Dehalogenase-type Phosphatases AUM and Chronophin Provide Insight into the Basis of Their Different Substrate SpecificitiesChronophin Dimerization Is Required for Proper Positioning of Its Substrate Specificity LoopStructure of the trehalose-6-phosphate phosphatase from Brugia malayi reveals key design principles for anthelmintic drugsHigh-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutasesA family of metal-dependent phosphatases implicated in metabolite damage-controlHomo sapiens dullard protein phosphatase shows a preference for the insulin-dependent phosphorylation site of lipin1Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatasesA MORN1-associated HAD phosphatase in the basal complex is essential for Toxoplasma gondii daughter buddingCatalytic DNA with phosphatase activityEnzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatasesReceiver domain structure and function in response regulator proteins.Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).New insights about enzyme evolution from large scale studies of sequence and structure relationships.Farnesyl phosphatase, a Corpora allata enzyme involved in juvenile hormone biosynthesis in Aedes aegypti.Genes and co-expression modules common to drought and bacterial stress responses in Arabidopsis and riceFunctional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Structure of Saccharomyces cerevisiae Rtr1 reveals an active site for an atypical phosphataseStructures of trehalose-6-phosphate phosphatase from pathogenic fungi reveal the mechanisms of substrate recognition and catalysisConsequences of domain insertion on sequence-structure divergence in a superfold.Co-evolution of HAD phosphatase and hotdog-fold thioesterase domain function in the menaquinone-pathway fusion proteins BF1314 and PG1653.Glycosides as compatible solutes: biosynthesis and applications.Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Toward mechanistic classification of enzyme functions.Human HAD phosphatases: structure, mechanism, and roles in health and disease.Specificity in transition state binding: the Pauling model revisited.Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis.An essential developmental function for murine phosphoglycolate phosphatase in safeguarding cell proliferationCap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1Crystallization and preliminary X-ray analysis of mannosyl-3-phosphoglycerate phosphatase from Thermus thermophilus HB27.Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific α-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations.Structure-guided approach for detecting large domain inserts in protein sequences as illustrated using the haloacid dehalogenase superfamily.A common structural scaffold in CTD phosphatases that supports distinct catalytic mechanisms.Measurement of Enzyme Activities.
P2860
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P2860
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
Markers of fitness in a successful enzyme superfamily.
@en
Markers of fitness in a successful enzyme superfamily.
@nl
type
label
Markers of fitness in a successful enzyme superfamily.
@en
Markers of fitness in a successful enzyme superfamily.
@nl
prefLabel
Markers of fitness in a successful enzyme superfamily.
@en
Markers of fitness in a successful enzyme superfamily.
@nl
P2860
P1476
Markers of fitness in a successful enzyme superfamily.
@en
P2093
Karen N Allen
P2860
P304
P356
10.1016/J.SBI.2009.09.008
P577
2009-11-02T00:00:00Z