Probing the specificity of a trypanosomal aromatic α-hydroxy acid dehydrogenase by site-directed mutagenesis

Javier Vernal; András Fiser; Andrej Šali; Miklós Müller; Juan José Cazzulo; Cristina Nowicki

doi:10.1016/s0006-291x(02)00270-x

journal article Open Access Apr 01, 2002

Probing the specificity of a trypanosomal aromatic α-hydroxy acid dehydrogenase by site-directed mutagenesis

Javier Vernal András Fiser

Andrej Šali

Miklós Müller Juan José Cazzulo Cristina Nowicki

Biochemical and Biophysical Research Communications Vol. 293 No. 1 pp. 633-639 · Elsevier BV

View at Publisher Save 10.1016/s0006-291x(02)00270-x

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References

35

[1]

Goward "Malate dehydrogenase: a model for structure, evolution, and catalysis" Protein Sci. (1994) 10.1002/pro.5560031027

[2]

Golding "The structural basis of molecular adaptation" Mol. Biol. Evol. (1998) 10.1093/oxfordjournals.molbev.a025932

[3]

Montemartini "Purification and partial structural and kinetic characterization of an aromatic l-alpha-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi" Mol. Biochem. Parasitol. (1994) 10.1016/0166-6851(94)00145-6

[4]

Cazzulo Franke "The NAD-linked aromatic α-hydroxy acid dehydrogenase from Trypanosoma cruzi: a new member of the cytosolic malate dehydrogenase group without malate dehydrogenase activity" Eur. J. Biochem. (1999) 10.1046/j.1432-1327.1999.00926.x

[5]

Vernal "Sequencing and heterologous expression of a cytosolic-type malate dehydrogenase of Trypanosoma brucei" Mol. Biochem. Parasitol. (2001) 10.1016/s0166-6851(01)00343-7

[6]

Uttaro "A family of highly conserved glycosomal 2-hydroxyacid dehydrogenases from Phytomonas sp" J. Biol. Chem. (2000) 10.1074/jbc.m006080200

[7]

Baernstein "Lactic dehydrogenase in Trichomonas vaginalis" J. Parasitol. (1959) 10.2307/3274564

[8]

Harmych "Lactate dehydrogenase from the protozoan parasite Trichomonas vaginalis" Comp. Biochem. Physiol. (1996) 10.1016/s0305-0491(96)00164-2

[9]

Wu "Convergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase" Proc. Natl. Acad. Sci. USA (1999) 10.1073/pnas.96.11.6285

[10]

Montemartini "Production of aromatic alpha-hydroxyacids by epimastigotes of Trypanosoma cruzi, and its possible role in NADH reoxidation" FEMS Microbiol. Lett. (1994)

[11]

Eventoff "Structural adaptations of lactate dehydrogenase isoenzymes" Proc. Natl. Acad. Sci. USA (1977) 10.1073/pnas.74.7.2677

[12]

Birktoft "Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase" Proc. Natl. Acad. Sci. USA (1982) 10.1073/pnas.79.20.6166

[13]

Birktoft "Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-Å resolution" Biochemistry (1989) 10.1021/bi00440a051

[14]

McAlister Henn "Evolutionary relationships among the malate dehydrogenases" Trends Biochem. Sci. (1988) 10.1016/0968-0004(88)90146-6

[15]

Nicholls "The importance of arginine 102 for the substrate specificity of Escherichia coli malate dehydrogenase" Biochem. Biophys. Res. Commun. (1992) 10.1016/0006-291x(92)92311-k

[16]

Birktoft "Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies" Biochemistry (1987) 10.1021/bi00384a011

[17]

Hall "Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase, citrate and NAD at 1.9 Å resolution" J. Mol. Biol. (1993) 10.1006/jmbi.1993.1377

[18]

Nicholls "Substitution of the amino acid at position 102 with polar and aromatic residues influences substrate specificity of lactate dehydrogenases" J. Protein Chem. (1994) 10.1007/bf01892000

[19]

Clarke "Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity" Biochem. Biophys. Res. Commun. (1987) 10.1016/0006-291x(87)91070-9

[20]

Wilks "A specific highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework" Science (1988) 10.1126/science.3201242

[21]

Cendrin "Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui" Biochemistry (1993) 10.1021/bi00067a020

[22]

Boernke "Stringency of substrate specificity of Escherichia coli malate dehydrogenase" Arch. Biochem. Biophys. (1995) 10.1006/abbi.1995.1434

[23]

Cordwell "Malate/lactate dehydrogenase in mollicutes: evidence for a multienzyme protein" Gene (1997) 10.1016/s0378-1119(97)00063-2

[24]

Lee "Crystal structure of the MJ0490 gene product of the hyperthermophylic archaebacterium Methanococcus jannaschii a novel member of the lactate/malate family of dehydrogenases" J. Mol. Biol. (2001) 10.1006/jmbi.2001.4532

[25]

Comparative Protein Modelling by Satisfaction of Spatial Restraints

Andrej Šali, Tom L. Blundell

Journal of Molecular Biology 1998 10.1006/jmbi.1993.1626

[26]

Recognition of errors in three‐dimensional structures of proteins

Manfred J. Sippl

Proteins: Structure, Function, and Bioinformatics 1993 10.1002/prot.340170404

[27]

PROCHECK: a program to check the stereochemical quality of protein structures

R. A. Laskowski, M. W. MacArthur, D. S. Moss et al.

Journal of Applied Crystallography 1993 10.1107/s0021889892009944

[28]

Iterated profile searches with PSI-BLAST—a tool for discovery in protein databases

Stephen F. Altschul, Eugene V. Koonin

Trends in Biochemical Sciences 2000 10.1016/s0968-0004(98)01298-5

[29]

Modeling of loops in protein structures

András Fiser, Richard Kinh Gian Do, Andrej Šali

Protein Science 2000 10.1110/ps.9.9.1753

[30]

Fraser "The use of least squares in data analysis" (1973)

[31]

Bradford "A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding" Anal. Biochem. (1976) 10.1016/0003-2697(76)90527-3

[32]

Wright "From malate dehydrogenase to phenyllactate dehydrogenase. Incorporation of unnatural amino acids to generate an improved enzyme-catalyzed activity" J. Biol. Chem. (2000) 10.1074/jbc.m003652200

[33]

Birktoft "The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase" J. Biol. Chem. (1983) 10.1016/s0021-9258(18)33280-0

[34]

Müller "Biochemistry of Trichomonas vaginalis" (1989)

[35]

Ryley "Studies on the metabolism of the protozoa. Metabolism of the parasitic flagellate Trichomonas foetus" Biochem. J. (1955) 10.1042/bj0590361

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References

Details

Published: Apr 01, 2002
Vol/Issue: 293(1)
Pages: 633-639
License: View

Authors

Laboratories of Molecular Biophysics, Pels Family Center for Biochemistry and Structural Biology, Rockefeller University, 1230 York Ave, New York, NY 10021;

QB3

Funding

National Institutes of Health

U.S. Public Health Service

Agencia Nacional de Promoción Científica y Tecnológica

Styrelsen för Internationellt Utvecklingssamarbete

Cite This Article

Javier Vernal, András Fiser, Andrej Šali, et al. (2002). Probing the specificity of a trypanosomal aromatic α-hydroxy acid dehydrogenase by site-directed mutagenesis. Biochemical and Biophysical Research Communications, 293(1), 633-639. https://doi.org/10.1016/s0006-291x(02)00270-x

Probing the specificity of a trypanosomal aromatic α-hydroxy acid dehydrogenase by site-directed mutagenesis

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