His-404 and His-405 are Essential for Enzyme Catalytic Activities of a Bacterial Indole-3-Acetyl-l-Aspartic Acid Hydrolase
Author:
Publisher
Oxford University Press (OUP)
Subject
Cell Biology,Plant Science,Physiology,General Medicine
Link
http://academic.oup.com/pcp/article-pdf/45/9/1335/19669828/pch153.pdf
Reference17 articles.
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2. Bartel, B. and Fink, G.R. (1995) ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates. Science268: 1745–1748.
3. Bialek, K. and Cohen, J.D. (1986) Isolation and partial characterization of the major amide-linked conjugate of indole-3-acetic acid from Phaselous vulgaris L. Plant Physiol.80: 99–104.
4. Chou, J.C., Kuleck, G.A., Cohen, J.D. and Mulbry, W.W. (1996) Partial purification and characterization of an inducible indole-3-acetyl-l-aspartic acid hydrolase from Enterobacter agglomerans. Plant Physiol.112: 1281–1287.
5. Chou, J.C., Mulbry, W.W. and Cohen, J.D. (1998) The gene for indole-3-acetyl-l-aspartic acid hydrolase from Enterobacter agglomerans: molecular cloning, nucleotide sequence, and expression in Escherichia coli. Mol. Gen. Genet.259: 172–178.
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