NDLI: The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.

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The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.

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The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Barber, M. J. Ferreira, G. C. Tan, D.
Description	Country affiliation: United States Author Affiliation: Tan D ( Department of Biochemistry and Molecular Biology, College of Medicine, University of South Florida, Tampa 33612, USA.)
Abstract	5-Aminolevulinate synthase (EC 2.3.1.37) is the first enzyme in the heme biosynthesis in nonplant eukaryotes and some prokaryotes. It functions as a homodimer and requires pyridoxal 5'-phosphate as an essential cofactor. Tyr-121 is a conserved residue in all known sequences of 5-aminolevulinate synthases. Further, it corresponds to Tyr-70 of Escherichia coli aspartate aminotransferase, which has been shown to interact with the cofactor and prevent the dissociation of the cofactor from the enzyme. To test whether Tyr-121 is involved in cofactor binding in murine erythroid 5-aminolevulinate synthase, Tyr-121 of murine erythroid 5-aminolevulinate synthase was substituted by Phe and His using site-directed mutagenesis. The Y121F mutant retained 36% of the wild-type activity and the Km value for substrate glycine increased 34-fold, while the activity of the Y121H mutant decreased to 5% of the wild-type activity and the Km value for glycine increased fivefold. The pKa1 values in the pH-activity profiles of the wild-type and mutant enzymes were 6.41, 6.54, and 6.65 for wild-type, Y121F, and Y121H, respectively. The UV-visible and CD spectra of Y121F and Y121H mutants were similar to those of the wild-type with the exception of an absorption maximum shift (420 --> 395 nm) for the Y121F mutant in the visible spectrum region, suggesting that the cofactor binds the Y121F mutant enzyme in a more unrestrained manner. Y121F and Y121H mutant enzymes also exhibited lower affinity than the wild-type for the cofactor, reflected in the Kd values for pyridoxal 5'-phosphate (26.5, 6.75, and 1.78 microM for Y121F, Y121H, and the wild-type, respectively). Further, Y121F and Y121H proved less thermostable than the wild type. Taken together, these findings indicate that Tyr-121 plays a critical role in cofactor binding of murine erythroid 5-aminolevulinate synthase.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	5-aminolevulinate Synthetase Metabolism Coenzymes Tyrosine Chemistry Genetics Amino Acid Sequence Animals Circular Dichroism Enzyme Stability Kinetics Mice Molecular Sequence Data Mutagenesis Protein Binding Sequence Alignment Spectrophotometry, Ultraviolet Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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