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- Albalat R., González-Duarte, Atrian S. Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme. FEBS Lett. 1992 Aug 24;308(3):235–239. doi: 10.1016/0014-5793(92)81282-q. [DOI] [PubMed] [Google Scholar]
- Baker M. E. Evolution of enzymatic regulation of prostaglandin action: novel connections to regulation of human sex and adrenal function, antibiotic synthesis and nitrogen fixation. Prostaglandins. 1991 Nov;42(5):391–410. doi: 10.1016/0090-6980(91)90031-a. [DOI] [PubMed] [Google Scholar]
- Baker M. E. Evolution of regulation of steroid-mediated intercellular communication in vertebrates: insights from flavonoids, signals that mediate plant-rhizobia symbiosis. J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):301–308. doi: 10.1016/0960-0760(92)90355-m. [DOI] [PubMed] [Google Scholar]
- Baker M. E. Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: functional diversity from two ancestral dehydrogenases. Steroids. 1991 Jul;56(7):354–360. doi: 10.1016/0039-128x(91)90067-6. [DOI] [PubMed] [Google Scholar]
- Baker M. E. Sequence analysis of steroid- and prostaglandin-metabolizing enzymes: application to understanding catalysis. Steroids. 1994 Apr;59(4):248–258. doi: 10.1016/0039-128x(94)90109-0. [DOI] [PubMed] [Google Scholar]
- Baker M. E. Similarities between legume-rhizobium communication and steroid-mediated intercellular communication in vertebrates. Can J Microbiol. 1992 Jun;38(6):541–547. doi: 10.1139/m92-089. [DOI] [PubMed] [Google Scholar]
- Benli M., Schulz R., Apel K. Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana. Plant Mol Biol. 1991 Apr;16(4):615–625. doi: 10.1007/BF00023426. [DOI] [PubMed] [Google Scholar]
- Chen Z., Jiang J. C., Lin Z. G., Lee W. R., Baker M. E., Chang S. H. Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry. 1993 Apr 6;32(13):3342–3346. doi: 10.1021/bi00064a017. [DOI] [PubMed] [Google Scholar]
- Chen Z., Lee W. R., Chang S. H. Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase. Eur J Biochem. 1991 Dec 5;202(2):263–267. doi: 10.1111/j.1432-1033.1991.tb16371.x. [DOI] [PubMed] [Google Scholar]
- Chen Z., Lu L., Shirley M., Lee W. R., Chang S. H. Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase. Biochemistry. 1990 Feb 6;29(5):1112–1118. doi: 10.1021/bi00457a003. [DOI] [PubMed] [Google Scholar]
- Darrah P. M., Kay S. A., Teakle G. R., Griffiths W. T. Cloning and sequencing of protochlorophyllide reductase. Biochem J. 1990 Feb 1;265(3):789–798. doi: 10.1042/bj2650789. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dayhoff M. O., Barker W. C., Hunt L. T. Establishing homologies in protein sequences. Methods Enzymol. 1983;91:524–545. doi: 10.1016/s0076-6879(83)91049-2. [DOI] [PubMed] [Google Scholar]
- DeLong A., Calderon-Urrea A., Dellaporta S. L. Sex determination gene TASSELSEED2 of maize encodes a short-chain alcohol dehydrogenase required for stage-specific floral organ abortion. Cell. 1993 Aug 27;74(4):757–768. doi: 10.1016/0092-8674(93)90522-r. [DOI] [PubMed] [Google Scholar]
- Ensor C. M., Tai H. H. Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem Biophys Res Commun. 1991 Apr 30;176(2):840–845. doi: 10.1016/s0006-291x(05)80262-1. [DOI] [PubMed] [Google Scholar]
- Feng D. F., Doolittle R. F. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 1990;183:375–387. doi: 10.1016/0076-6879(90)83025-5. [DOI] [PubMed] [Google Scholar]
- Ghosh D., Weeks C. M., Grochulski P., Duax W. L., Erman M., Rimsay R. L., Orr J. C. Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10064–10068. doi: 10.1073/pnas.88.22.10064. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Griffiths W. T. Protochlorophyll and protochlorophyllide as precursors for chlorophyll synthesis in vitro. FEBS Lett. 1974 Dec 15;49(2):196–200. doi: 10.1016/0014-5793(74)80510-7. [DOI] [PubMed] [Google Scholar]
- Grimshaw C. E., Matthews D. A., Varughese K. I., Skinner M., Xuong N. H., Bray T., Hoch J., Whiteley J. M. Characterization and nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37-isoleucine replacement. J Biol Chem. 1992 Aug 5;267(22):15334–15339. [PubMed] [Google Scholar]
- Krook M., Ghosh D., Strömberg R., Carlquist M., Jörnvall H. Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):502–506. doi: 10.1073/pnas.90.2.502. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krozowski Z. 11 beta-hydroxysteroid dehydrogenase and the short-chain alcohol dehydrogenase (SCAD) superfamily. Mol Cell Endocrinol. 1992 Mar;84(1-2):C25–C31. doi: 10.1016/0303-7207(92)90064-d. [DOI] [PubMed] [Google Scholar]
- Obeid J., White P. C. Tyr-179 and Lys-183 are essential for enzymatic activity of 11 beta-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun. 1992 Oct 15;188(1):222–227. doi: 10.1016/0006-291x(92)92373-6. [DOI] [PubMed] [Google Scholar]
- Oliver R. P., Griffiths W. T. Covalent labelling of the NADPH: protochlorophyllide oxidoreductase from etioplast membranes with [3H]N-phenylmaleimide. Biochem J. 1981 Apr 1;195(1):93–101. doi: 10.1042/bj1950093. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Persson B., Krook M., Jörnvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur J Biochem. 1991 Sep 1;200(2):537–543. doi: 10.1111/j.1432-1033.1991.tb16215.x. [DOI] [PubMed] [Google Scholar]
- Schulz R., Steinmüller K., Klaas M., Forreiter C., Rasmussen S., Hiller C., Apel K. Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. Mol Gen Genet. 1989 Jun;217(2-3):355–361. doi: 10.1007/BF02464904. [DOI] [PubMed] [Google Scholar]
- Scrutton N. S., Berry A., Perham R. N. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature. 1990 Jan 4;343(6253):38–43. doi: 10.1038/343038a0. [DOI] [PubMed] [Google Scholar]
- Slabas A. R., Chase D., Nishida I., Murata N., Sidebottom C., Safford R., Sheldon P. S., Kekwick R. G., Hardie D. G., Mackintosh R. W. Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein) reductase. Sequence identities with the nodG-gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti. Biochem J. 1992 Apr 15;283(Pt 2):321–326. doi: 10.1042/bj2830321. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spano A. J., He Z., Michel H., Hunt D. F., Timko M. P. Molecular cloning, nuclear gene structure, and developmental expression of NADPH: protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol Biol. 1992 Mar;18(5):967–972. doi: 10.1007/BF00019210. [DOI] [PubMed] [Google Scholar]
- Spano A. J., He Z., Timko M. P. NADPH: protochlorophyllide oxidoreductases in white pine (Pinus strobus) and loblolly pine (P. taeda). Evidence for light and developmental regulation of expression and conservation in gene organization and protein structure between angiosperms and gymnosperms. Mol Gen Genet. 1992 Dec;236(1):86–95. [PubMed] [Google Scholar]
- Tanaka M., Ohno S., Adachi S., Nakajin S., Shinoda M., Nagahama Y. Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J Biol Chem. 1992 Jul 5;267(19):13451–13455. [PubMed] [Google Scholar]
- Tannin G. M., Agarwal A. K., Monder C., New M. I., White P. C. The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization. J Biol Chem. 1991 Sep 5;266(25):16653–16658. [PubMed] [Google Scholar]
- Varughese K. I., Skinner M. M., Whiteley J. M., Matthews D. A., Xuong N. H. Crystal structure of rat liver dihydropteridine reductase. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6080–6084. doi: 10.1073/pnas.89.13.6080. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wermuth B. NADP-dependent 15-hydroxyprostaglandin dehydrogenase is homologous to NAD-dependent 15-hydroxyprostaglandin dehydrogenase and other short-chain alcohol dehydrogenases. Prostaglandins. 1992 Jul;44(1):5–9. doi: 10.1016/0090-6980(92)90102-y. [DOI] [PubMed] [Google Scholar]