Focus on O-phosphohydroxylysine, O-phosphohydroxyproline, N 1 -phosphotryptophan and S-phosphocysteine
The synthesis and chemistry of the lesser-known phosphoamino acids, O-phosphohydroxylysine, O-phosphohydroxyproline, N -phosphotryptophan and S-phosphocysteine are described in detail. In addition, where anything at all is known, the biological synthesis, occurrence and functions of these phosphoami...
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Veröffentlicht in: | Amino acids 2017-08, Vol.49 (8), p.1309-1323 |
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container_title | Amino acids |
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creator | Piggott, Matthew J Attwood, Paul V |
description | The synthesis and chemistry of the lesser-known phosphoamino acids, O-phosphohydroxylysine, O-phosphohydroxyproline, N
-phosphotryptophan and S-phosphocysteine are described in detail. In addition, where anything at all is known, the biological synthesis, occurrence and functions of these phosphoamino acids are described. Of these phosphoamino acids, only N
-phosphotryptophan has not been reported to occur in proteins; however, apart from the roles of S-phosphocysteine in the sugar transporter component (EII) and in catalysis by protein phosphotyrosine phosphatase, little is currently known about the biological roles of the phosphoamino acids when they occur as post-translational modifications. |
doi_str_mv | 10.1007/s00726-017-2446-x |
format | Article |
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-phosphotryptophan has not been reported to occur in proteins; however, apart from the roles of S-phosphocysteine in the sugar transporter component (EII) and in catalysis by protein phosphotyrosine phosphatase, little is currently known about the biological roles of the phosphoamino acids when they occur as post-translational modifications.</description><subject>Animals</subject><subject>Cysteine - analogs & derivatives</subject><subject>Cysteine - chemistry</subject><subject>Humans</subject><subject>Hydroxylysine - analogs & derivatives</subject><subject>Hydroxylysine - chemistry</subject><subject>Phosphoamino Acids - chemistry</subject><subject>Phosphorylation</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins - chemistry</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkMFOwzAMhiMEYmPwAFxQjxwIxKnTJkc0MUCa2IHdozZNtaGuKU0rrW9PRjcuHGxL9u9f9kfILbBHYCx98iHxhDJIKUdM6P6MTAFjSTkodU6mTMWKIgqYkCvvvxgDLiG5JBMuRSoFwykpF870PnJ1tKLNxvkQm6Fo3X6oBr-t7cO_ftO66nfwEUF0mnXt0HSu2WR1lNVF9Hnqm8F3NqivyUWZVd7eHOuMrBcv6_kbXa5e3-fPS2p4DB21XDJTyJILg3Fepphzk6XKSM4LgQpVDmkhUYHA8EmeQMxzzIQ1JZdYsHhG7kfbcOR3b32nd1tvbFVltXW916BYAhhY8SCFUWpa531rS920213WDhqYPtDVI10d6OoDXb0PO3dH-z7f2eJv44Qz_gGDs3cd</recordid><startdate>201708</startdate><enddate>201708</enddate><creator>Piggott, Matthew J</creator><creator>Attwood, Paul V</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201708</creationdate><title>Focus on O-phosphohydroxylysine, O-phosphohydroxyproline, N 1 -phosphotryptophan and S-phosphocysteine</title><author>Piggott, Matthew J ; Attwood, Paul V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c231t-e280cd8f25c43bf74b2ca79c822d54949b17d849154281b6132b4a5ecf284d03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Cysteine - analogs & derivatives</topic><topic>Cysteine - chemistry</topic><topic>Humans</topic><topic>Hydroxylysine - analogs & derivatives</topic><topic>Hydroxylysine - chemistry</topic><topic>Phosphoamino Acids - chemistry</topic><topic>Phosphorylation</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Piggott, Matthew J</creatorcontrib><creatorcontrib>Attwood, Paul V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Piggott, Matthew J</au><au>Attwood, Paul V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Focus on O-phosphohydroxylysine, O-phosphohydroxyproline, N 1 -phosphotryptophan and S-phosphocysteine</atitle><jtitle>Amino acids</jtitle><addtitle>Amino Acids</addtitle><date>2017-08</date><risdate>2017</risdate><volume>49</volume><issue>8</issue><spage>1309</spage><epage>1323</epage><pages>1309-1323</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>The synthesis and chemistry of the lesser-known phosphoamino acids, O-phosphohydroxylysine, O-phosphohydroxyproline, N
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-phosphotryptophan has not been reported to occur in proteins; however, apart from the roles of S-phosphocysteine in the sugar transporter component (EII) and in catalysis by protein phosphotyrosine phosphatase, little is currently known about the biological roles of the phosphoamino acids when they occur as post-translational modifications.</abstract><cop>Austria</cop><pmid>28578504</pmid><doi>10.1007/s00726-017-2446-x</doi><tpages>15</tpages></addata></record> |
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source | MEDLINE; Springer Nature - Complete Springer Journals |
subjects | Animals Cysteine - analogs & derivatives Cysteine - chemistry Humans Hydroxylysine - analogs & derivatives Hydroxylysine - chemistry Phosphoamino Acids - chemistry Phosphorylation Protein Processing, Post-Translational Proteins - chemistry |
title | Focus on O-phosphohydroxylysine, O-phosphohydroxyproline, N 1 -phosphotryptophan and S-phosphocysteine |
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