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Crystal structure of common type acylphosphatase from bovine testis
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title
Crystal structure of common type acylphosphatase from bovine testis
(English)
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main subject
crystal structure
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Acylphosphatase
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author name string
M M Thunnissen
series ordinal
1
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N Taddei
series ordinal
2
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G Liguri
series ordinal
3
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G Ramponi
series ordinal
4
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P Nordlund
series ordinal
5
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publication date
15 January 1997
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published in
Structure
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volume
5
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issue
1
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page(s)
69-79
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cites work
Acylphosphatase induced modifications in the functional properties of erythrocyte membrane sodium pump
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Effect of exogenously added acylphosphatases on inositol lipid metabolism in human platelets.
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A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure
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Purification and properties of porcine testis acylphosphatase.
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Distribution and classification of acylphosphatase isozymes
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Bovine testis acylphosphatase: purification and amino acid sequence.
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The structure and properties of horse muscle acylphosphatase in solution. Mobility of antigenic and active site regions
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Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity
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The NMR structure of the activation domain isolated from porcine procarboxypeptidase B
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Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
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Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A
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Crystal structure of a prokaryotic ribosomal protein
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Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution
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Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein
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Kinetic studies with muscle acylphosphatase.
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Arginine-23 is involved in the catalytic site of muscle acylphosphatase.
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Properties of N-terminus truncated and C-terminus mutated muscle acylphosphatases.
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C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation.
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Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46.
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The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
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Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis.
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Crystallisation and preliminary X-ray analysis of the 'common-type' acylphosphatase.
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Identifiers
DOI
10.1016/S0969-2126(97)00167-6
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Fatcat ID
release_bzbrlfxekzcs5iuotgsbmi5ad4
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PubMed publication ID
9016712
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