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The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: Multiple forced covariant amino acid substitutions in natural variants
Open accessAbstract
The role of the Lys68*Residues pertaining to the opposite subunit. :Glu265 intersubunit salt bridge that is conserved (Csb) in all known aspartate aminotransferases (AATases), except those of animal cytosolic, Ac (His68*:Glu265), and plant mitochondrial, Pm (Met68*:Gln265), origins, was evaluated in the Escherichia coli AATase. Two double‐mutant cycles, to K68M/E265Q and the charge reversed K68E/E265K, were characterized with the context dependence (C) and impact (I) formalism, previously defined for functional chimeric analysis. Mutations of Lys68* with Glu265 fixed are generally more deleterious than the converse mutations of Glu265 with Lys68* fixed, showing that buried negative charges have greater effects than buried positive charges in this context. Replacement of the charged Lys68*:Glu265 with the K68M/E265Q neutral pair introduces relatively small effects on the kinetic parameters. The differential sensitivity of kcat/KM, L‐Asp and kcat/KM, α‐KG to salt bridge mutagenic replacements is shown by a linear‐free energy relationship, in which the logarithms of the latter second order rate constants are generally decreased by a factor of two more than are those of the former. Thus, kcat/KM, L‐Asp and kcat/KM, α‐KG are 133 and 442 mM−1 s−1 for the wild‐type (WT) enzyme, respectively, but their relative order is reversed in the more severely compromised mutants (14.8 and 5.3 mM−1 s−1 for K68E). A Venn diagram illustrates apparent forced covariances of groups of amino acids that accompany the naturally occurring salt bridge replacements in the Pm and Ac classes. The more deeply rooted tree indicates that the Csb variant was the ancestral specie.
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“Before and after nitrogen upshift, AST's two substrate binding sites (one for the four carbon compounds oxaloacetate and aspartate, and the other for the five carbon compounds glutamate and α-ketoglutarate) are both saturated, largely with aspartate and glutamate (Powell and Morrison, 1978; Deu et al, 2002).”
From Metabolomics-driven quantitative analysis of ammonia assimilation in E. coli (2009) · cites this paper as Deu et al, 2002
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Metabolomics-driven quantitative analysis of ammonia assimilation in E. coli
Yuan, J., Doucette, C. D., Fowler, W. U., Feng, X., Piazza, M., Rabitz, H. A., Wingreen, N. S., & Rabinowitz, J. D. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.60 · Cited by 178
Metadata
- Authors
- Deu, E., Koch, K. A., & Kirsch, J. F.
- Affiliations
- University of California, Berkeley (US)
- Triad National Security (United States) (US)
- Corresponding author
- Kirsch, Jack F.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2002-05
- Volume
- 11
- Issue
- 5
- Pages
- 1062-1073
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC2373551
- OpenAlex
- W2034621068
- Cited by
- 15
- References
- 37
- Citations by year
- 2021: 1 · 2019: 1 · 2016: 1 · 2013: 3
- FWCI
- 0.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Protein Science (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM35393, F32GM020585, R01GM035393, GM 20585)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- aspartate aminotransferase, enzyme kinetics, double mutant cycles, context sensitivity, linear free energy relationships, natural variants, Escherichia coli enzyme, ancestral state reconstruction
- MeSH terms
- Amino Acid Sequence, Aspartate Aminotransferases, Kinetics, Models, Biological, Molecular Sequence Data, Phylogeny, Substrate Specificity, Sequence Alignment, Amino Acid Substitution, Protein Structure, Quaternary
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