Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein
about
Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzymeA Sweet Spot for Molecular Diagnostics: Coupling Isothermal Amplification and Strand Exchange Circuits to GlucometersProbing the active site of Corynebacterium callunae starch phosphorylase through the characterization of wild-type and His334-->Gly mutant enzymes.The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose.Catalytic mechanism of alpha-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants.
P2860
Thermal denaturation pathway of starch phosphorylase from Corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
Thermal denaturation pathway o ...... dimer structure of the protein
@en
Thermal denaturation pathway o ...... dimer structure of the protein
@nl
type
label
Thermal denaturation pathway o ...... dimer structure of the protein
@en
Thermal denaturation pathway o ...... dimer structure of the protein
@nl
prefLabel
Thermal denaturation pathway o ...... dimer structure of the protein
@en
Thermal denaturation pathway o ...... dimer structure of the protein
@nl
P2093
P2860
P356
P1433
P1476
Thermal denaturation pathway o ...... dimer structure of the protein
@en
P2093
Griessler R
Nidetzky B
P2860
P304
P356
10.1110/PS.9.6.1149
P577
2000-06-01T00:00:00Z