{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T01:33:45Z","timestamp":1785288825587,"version":"3.55.0"},"reference-count":55,"publisher":"National Academy of Sciences","issue":"47","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2007,11,20]]},"abstract":"<jats:p>\n                    Members of the nitrilase 4 (NIT4) family of higher plants catalyze the conversion of \u03b2-cyanoalanine to aspartic acid and asparagine, a key step in cyanide detoxification. Grasses (Poaceae) possess two different NIT4 homologs (NIT4A and NIT4B), but none of the recombinant Poaceae enzymes analyzed showed activity with \u03b2-cyanoalanine, whereas protein extracts of the same plants clearly posses this activity.\n                    <jats:italic>Sorghum bicolor<\/jats:italic>\n                    contains three NIT4 isoforms\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4A,\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4B1, and\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4B2. Individually, each isoform does not possess enzymatic activity whereas the heteromeric complexes\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4A\/B1 and\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4A\/B2 hydrolyze \u03b2-cyanoalanine with high activity. In addition, the\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4A\/B2 complex accepts additional substrates, the best being 4-hydroxyphenylacetonitrile. Corresponding NIT4A and NIT4B isoforms from other Poaceae species can functionally complement the sorghum isoforms in these complexes. Site-specific mutagenesis of the active site cysteine residue demonstrates that hydrolysis of \u03b2-cyanoalanine is catalyzed by the NIT4A isoform in both complexes whereas hydrolysis of 4-hydroxyphenylacetonitrile occurs at the NIT4B2 isoform. 4-Hydroxyphenylacetonitrile was shown to be an\n                    <jats:italic>in vitro<\/jats:italic>\n                    breakdown product of the cyanogenic glycoside dhurrin, a main constituent in\n                    <jats:italic>S. bicolor<\/jats:italic>\n                    . The results indicate that the\n                    <jats:italic>Sb<\/jats:italic>\n                    NIT4A\/B2 heterocomplex plays a key role in an endogenous turnover of dhurrin proceeding via 4-hydroxyphenylacetonitrile and thereby avoiding release of toxic hydrogen cyanide. The operation of this pathway would enable plants to use cyanogenic glycosides as transportable and remobilizable nitrogenous storage compounds. Through combinatorial biochemistry and neofunctionalizations, the small family of nitrilases has gained diverse biological functions in nitrile metabolism.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0709315104","type":"journal-article","created":{"date-parts":[[2007,11,14]],"date-time":"2007-11-14T21:19:01Z","timestamp":1195075141000},"page":"18848-18853","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":104,"title":["Evolution of heteromeric nitrilase complexes in Poaceae with new functions in nitrile metabolism"],"prefix":"10.1073","volume":"104","author":[{"given":"Roland","family":"Jenrich","sequence":"first","affiliation":[{"name":"*Department of Plant Physiology, Ruhr-Universit\u00e4t Bochum, 44801 Bochum, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inga","family":"Trompetter","sequence":"additional","affiliation":[{"name":"*Department of Plant Physiology, Ruhr-Universit\u00e4t Bochum, 44801 Bochum, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u00f8ren","family":"Bak","sequence":"additional","affiliation":[{"name":"Plant Biochemistry Laboratory, Department of Plant Biology, Center for Molecular Plant Physiology, University of Copenhagen, DK-1871 Frederiksberg C, Copenhagen, Denmark; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carl Erik","family":"Olsen","sequence":"additional","affiliation":[{"name":"Department of Natural Sciences, University of Copenhagen, DK-1871 Frederiksberg C, Copenhagen, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Birger Lindberg","family":"M\u00f8ller","sequence":"additional","affiliation":[{"name":"Plant Biochemistry Laboratory, Department of Plant Biology, Center for Molecular Plant Physiology, University of Copenhagen, DK-1871 Frederiksberg C, Copenhagen, Denmark; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Piotrowski","sequence":"additional","affiliation":[{"name":"*Department of Plant Physiology, Ruhr-Universit\u00e4t Bochum, 44801 Bochum, 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