Amino acid oxidases from microbial sources: types, properties, functions, and applications

L-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of L-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. L-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Beca...

Full description

Saved in:
Bibliographic Details
Published in:Applied microbiology and biotechnology 2014, Vol.98 (4), p.1507-1515
Main Authors: Hossain, Gazi Sakir, Li, Jianghua, Shin, Hyun-dong, Du, Guocheng, Liu, Long, Chen, Jian
Format: Article
Language:English
Subjects:
acids
adenine
amino acid metabolism
ammonia
antimicrobial properties
deamination
recombinant proteins
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 1515
container_issue 4
container_start_page 1507
container_title Applied microbiology and biotechnology
container_volume 98
creator Hossain, Gazi Sakir
Li, Jianghua
Shin, Hyun-dong
Du, Guocheng
Liu, Long
Chen, Jian
description L-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of L-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. L-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Because expressing LAAOs as recombinant proteins in heterologous hosts is difficult, their biotechnological applications have not been thoroughly advanced. LAAOs are thought to contribute to amino acid catabolism, enhance iron acquisition, display antimicrobial activity, and catalyze keto acid production, among other roles. Here, we review the types, properties, structures, biological functions, heterologous expression, and applications of LAAOs obtained from microbial sources. We expect this review to increase interest in LAAO studies.
format article
fullrecord <record><control><sourceid>fao</sourceid><recordid>TN_cdi_fao_agris_US201400042091</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>US201400042091</sourcerecordid><originalsourceid>FETCH-LOGICAL-f481-7f4cb1fbb574f3eace5e0d9eee6b85dd6a140561cd5afb2e07788ac7118029913</originalsourceid><addsrcrecordid>eNqFjMtKAzEYhYMoWKvPYB7AgSST27grxUuh4MK6cVP-JH8kMjMZkino21sve1fn4_Cdc0IWXLaiYZrLU7Jg3KjGqM6ek4ta3xnjwmq9IK-rIY2Zgk-B5o8UoGKlseSBDsmX7BL0tOZD8Vhv6fw5Yb2hU8kTljl9czyMfk55PCKMgcI09cnDT3NJziL0Fa_-ckl293e79WOzfXrYrFfbJkrLGxOldzw6p4yMLYJHhSx0iKidVSFo4JIpzX1QEJ1AZoy14A3nlomu4-2SXP_eRsh7eCup7l-eBTuuGJOC_WOI1irefgGmNla-</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Amino acid oxidases from microbial sources: types, properties, functions, and applications</title><source>ABI/INFORM Global</source><source>Springer Nature</source><creator>Hossain, Gazi Sakir ; Li, Jianghua ; Shin, Hyun-dong ; Du, Guocheng ; Liu, Long ; Chen, Jian</creator><creatorcontrib>Hossain, Gazi Sakir ; Li, Jianghua ; Shin, Hyun-dong ; Du, Guocheng ; Liu, Long ; Chen, Jian</creatorcontrib><description>L-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of L-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. L-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Because expressing LAAOs as recombinant proteins in heterologous hosts is difficult, their biotechnological applications have not been thoroughly advanced. LAAOs are thought to contribute to amino acid catabolism, enhance iron acquisition, display antimicrobial activity, and catalyze keto acid production, among other roles. Here, we review the types, properties, structures, biological functions, heterologous expression, and applications of LAAOs obtained from microbial sources. We expect this review to increase interest in LAAO studies.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><language>eng</language><publisher>Springer-Verlag</publisher><subject>acids ; adenine ; amino acid metabolism ; ammonia ; antimicrobial properties ; deamination ; recombinant proteins</subject><ispartof>Applied microbiology and biotechnology, 2014, Vol.98 (4), p.1507-1515</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,4010</link.rule.ids></links><search><creatorcontrib>Hossain, Gazi Sakir</creatorcontrib><creatorcontrib>Li, Jianghua</creatorcontrib><creatorcontrib>Shin, Hyun-dong</creatorcontrib><creatorcontrib>Du, Guocheng</creatorcontrib><creatorcontrib>Liu, Long</creatorcontrib><creatorcontrib>Chen, Jian</creatorcontrib><title>Amino acid oxidases from microbial sources: types, properties, functions, and applications</title><title>Applied microbiology and biotechnology</title><description>L-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of L-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. L-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Because expressing LAAOs as recombinant proteins in heterologous hosts is difficult, their biotechnological applications have not been thoroughly advanced. LAAOs are thought to contribute to amino acid catabolism, enhance iron acquisition, display antimicrobial activity, and catalyze keto acid production, among other roles. Here, we review the types, properties, structures, biological functions, heterologous expression, and applications of LAAOs obtained from microbial sources. We expect this review to increase interest in LAAO studies.</description><subject>acids</subject><subject>adenine</subject><subject>amino acid metabolism</subject><subject>ammonia</subject><subject>antimicrobial properties</subject><subject>deamination</subject><subject>recombinant proteins</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNqFjMtKAzEYhYMoWKvPYB7AgSST27grxUuh4MK6cVP-JH8kMjMZkino21sve1fn4_Cdc0IWXLaiYZrLU7Jg3KjGqM6ek4ta3xnjwmq9IK-rIY2Zgk-B5o8UoGKlseSBDsmX7BL0tOZD8Vhv6fw5Yb2hU8kTljl9czyMfk55PCKMgcI09cnDT3NJziL0Fa_-ckl293e79WOzfXrYrFfbJkrLGxOldzw6p4yMLYJHhSx0iKidVSFo4JIpzX1QEJ1AZoy14A3nlomu4-2SXP_eRsh7eCup7l-eBTuuGJOC_WOI1irefgGmNla-</recordid><startdate>2014</startdate><enddate>2014</enddate><creator>Hossain, Gazi Sakir</creator><creator>Li, Jianghua</creator><creator>Shin, Hyun-dong</creator><creator>Du, Guocheng</creator><creator>Liu, Long</creator><creator>Chen, Jian</creator><general>Springer-Verlag</general><scope>FBQ</scope></search><sort><creationdate>2014</creationdate><title>Amino acid oxidases from microbial sources: types, properties, functions, and applications</title><author>Hossain, Gazi Sakir ; Li, Jianghua ; Shin, Hyun-dong ; Du, Guocheng ; Liu, Long ; Chen, Jian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f481-7f4cb1fbb574f3eace5e0d9eee6b85dd6a140561cd5afb2e07788ac7118029913</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>acids</topic><topic>adenine</topic><topic>amino acid metabolism</topic><topic>ammonia</topic><topic>antimicrobial properties</topic><topic>deamination</topic><topic>recombinant proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hossain, Gazi Sakir</creatorcontrib><creatorcontrib>Li, Jianghua</creatorcontrib><creatorcontrib>Shin, Hyun-dong</creatorcontrib><creatorcontrib>Du, Guocheng</creatorcontrib><creatorcontrib>Liu, Long</creatorcontrib><creatorcontrib>Chen, Jian</creatorcontrib><collection>AGRIS</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hossain, Gazi Sakir</au><au>Li, Jianghua</au><au>Shin, Hyun-dong</au><au>Du, Guocheng</au><au>Liu, Long</au><au>Chen, Jian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid oxidases from microbial sources: types, properties, functions, and applications</atitle><jtitle>Applied microbiology and biotechnology</jtitle><date>2014</date><risdate>2014</risdate><volume>98</volume><issue>4</issue><spage>1507</spage><epage>1515</epage><pages>1507-1515</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>L-Amino acid oxidases (LAAOs), which catalyze the stereospecific oxidative deamination of L-amino acids to α-keto acids and ammonia, are flavin adenine dinucleotide-containing homodimeric proteins. L-Amino acid oxidases are widely distributed in diverse organisms and have a range of properties. Because expressing LAAOs as recombinant proteins in heterologous hosts is difficult, their biotechnological applications have not been thoroughly advanced. LAAOs are thought to contribute to amino acid catabolism, enhance iron acquisition, display antimicrobial activity, and catalyze keto acid production, among other roles. Here, we review the types, properties, structures, biological functions, heterologous expression, and applications of LAAOs obtained from microbial sources. We expect this review to increase interest in LAAO studies.</abstract><pub>Springer-Verlag</pub><tpages>9</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0175-7598
ispartof Applied microbiology and biotechnology, 2014, Vol.98 (4), p.1507-1515
issn 0175-7598
1432-0614
language eng
recordid cdi_fao_agris_US201400042091
source ABI/INFORM Global; Springer Nature
subjects acids
adenine
amino acid metabolism
ammonia
antimicrobial properties
deamination
recombinant proteins
title Amino acid oxidases from microbial sources: types, properties, functions, and applications
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T23%3A28%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-fao&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino%20acid%20oxidases%20from%20microbial%20sources:%20types,%20properties,%20functions,%20and%20applications&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Hossain,%20Gazi%20Sakir&rft.date=2014&rft.volume=98&rft.issue=4&rft.spage=1507&rft.epage=1515&rft.pages=1507-1515&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/&rft_dat=%3Cfao%3EUS201400042091%3C/fao%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-f481-7f4cb1fbb574f3eace5e0d9eee6b85dd6a140561cd5afb2e07788ac7118029913%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true