CobaltMaghrebV1, PubMed, Checkpoint, bibRecord, 000041

Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.

Identifieur interne : 000041 ( PubMed/Checkpoint ); précédent : 000040; suivant : 000042

Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.

Auteurs : Hajer Ben Hlima [Tunisie] ; Nushin Aghajari ; Mamdouh Ben Ali ; Richard Haser ; Samir Bejar

Source :

Journal of industrial microbiology & biotechnology [ 1476-5535 ] ; 2012.

RBID : pubmed:22139345

Descripteurs français

KwdFr :
- Aldose-ketose isomerases (), Aldose-ketose isomerases (génétique), Aldose-ketose isomerases (métabolisme), Alignement de séquences, Calcium (métabolisme), Cinétique, Cobalt (métabolisme), Données de séquences moléculaires, Modèles moléculaires, Mutagenèse dirigée, Mutation, Stabilité enzymatique, Streptomyces (enzymologie), Séquence d'acides aminés.
MESH :
- enzymologie : Streptomyces.
- génétique : Aldose-ketose isomerases.
- métabolisme : Aldose-ketose isomerases, Calcium, Cobalt.
- Aldose-ketose isomerases, Alignement de séquences, Cinétique, Données de séquences moléculaires, Modèles moléculaires, Mutagenèse dirigée, Mutation, Stabilité enzymatique, Séquence d'acides aminés.

English descriptors

KwdEn :
- Aldose-Ketose Isomerases (chemistry), Aldose-Ketose Isomerases (genetics), Aldose-Ketose Isomerases (metabolism), Amino Acid Sequence, Calcium (metabolism), Cobalt (metabolism), Enzyme Stability, Kinetics, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Sequence Alignment, Streptomyces (enzymology).
MESH :
- chemical , chemistry : Aldose-Ketose Isomerases.
- chemical , genetics : Aldose-Ketose Isomerases.
- chemical , metabolism : Aldose-Ketose Isomerases, Calcium, Cobalt.
- enzymology : Streptomyces.
- Amino Acid Sequence, Enzyme Stability, Kinetics, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Sequence Alignment.

Abstract

The role of two amino acid residues linked to the two catalytic histidines His54 and His220 in kinetics and physicochemical properties of the Streptomyces sp. SK glucose isomerase (SKGI) was investigated by site-directed mutagenesis and molecular modeling. Two single mutations, F53L and G219D, and a double mutation F53L/G219D was introduced into the xylA SKGI gene. The F53L mutation increases the thermostability and the catalytic efficiency and also slightly shifts the optimum pH from 6.5 to 7, but displays a profile being similar to that of the wild-type enzyme concerning the effect of various metal ions. The G219D mutant is resistant to calcium inhibition retaining about 80% of its residual activity in 10 mM Ca²⁺ instead of 10% for the wild-type. This variant is activated by Mn²⁺ ions, but not Co²⁺, as seen for the wild-type enzyme. It does not require the latter for its thermostability, but has its half-life time displaced from 50 to 20 min at 85°C. The double mutation F53L/G219D restores the thermostability as seen for the wild-type enzyme while maintaining the resistance to the calcium inhibition. Molecular modeling suggests that the increase in thermostability is due to new hydrophobic interactions stabilizing α2 helix and that the resistance to calcium inhibition is a result of narrowing the binding site of catalytic ion.

DOI: 10.1007/s10295-011-1061-1
PubMed: 22139345

Affiliations:

Tunisie

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000042
to stream PubMed, to step Curation: 000042

Links to Exploration step

pubmed:22139345

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.</title>
<author><name sortKey="Hlima, Hajer Ben" sort="Hlima, Hajer Ben" uniqKey="Hlima H" first="Hajer Ben" last="Hlima">Hajer Ben Hlima</name>
<affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Microorganismes et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, Route de Sidi Mansour Km 6, B.P 1177, 3018 Sfax, Tunisia.</nlm:affiliation>
<country xml:lang="fr">Tunisie</country>
<wicri:regionArea>Laboratoire de Microorganismes et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, Route de Sidi Mansour Km 6, B.P 1177, 3018 Sfax</wicri:regionArea>
<wicri:noRegion>3018 Sfax</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Aghajari, Nushin" sort="Aghajari, Nushin" uniqKey="Aghajari N" first="Nushin" last="Aghajari">Nushin Aghajari</name>
</author>
<author><name sortKey="Ali, Mamdouh Ben" sort="Ali, Mamdouh Ben" uniqKey="Ali M" first="Mamdouh Ben" last="Ali">Mamdouh Ben Ali</name>
</author>
<author><name sortKey="Haser, Richard" sort="Haser, Richard" uniqKey="Haser R" first="Richard" last="Haser">Richard Haser</name>
</author>
<author><name sortKey="Bejar, Samir" sort="Bejar, Samir" uniqKey="Bejar S" first="Samir" last="Bejar">Samir Bejar</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2012">2012</date>
<idno type="RBID">pubmed:22139345</idno>
<idno type="pmid">22139345</idno>
<idno type="doi">10.1007/s10295-011-1061-1</idno>
<idno type="wicri:Area/PubMed/Corpus">000042</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000042</idno>
<idno type="wicri:Area/PubMed/Curation">000042</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000042</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000042</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000042</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.</title>
<author><name sortKey="Hlima, Hajer Ben" sort="Hlima, Hajer Ben" uniqKey="Hlima H" first="Hajer Ben" last="Hlima">Hajer Ben Hlima</name>
<affiliation wicri:level="1"><nlm:affiliation>Laboratoire de Microorganismes et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, Route de Sidi Mansour Km 6, B.P 1177, 3018 Sfax, Tunisia.</nlm:affiliation>
<country xml:lang="fr">Tunisie</country>
<wicri:regionArea>Laboratoire de Microorganismes et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, Route de Sidi Mansour Km 6, B.P 1177, 3018 Sfax</wicri:regionArea>
<wicri:noRegion>3018 Sfax</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Aghajari, Nushin" sort="Aghajari, Nushin" uniqKey="Aghajari N" first="Nushin" last="Aghajari">Nushin Aghajari</name>
</author>
<author><name sortKey="Ali, Mamdouh Ben" sort="Ali, Mamdouh Ben" uniqKey="Ali M" first="Mamdouh Ben" last="Ali">Mamdouh Ben Ali</name>
</author>
<author><name sortKey="Haser, Richard" sort="Haser, Richard" uniqKey="Haser R" first="Richard" last="Haser">Richard Haser</name>
</author>
<author><name sortKey="Bejar, Samir" sort="Bejar, Samir" uniqKey="Bejar S" first="Samir" last="Bejar">Samir Bejar</name>
</author>
</analytic>
<series><title level="j">Journal of industrial microbiology & biotechnology</title>
<idno type="eISSN">1476-5535</idno>
<imprint><date when="2012" type="published">2012</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldose-Ketose Isomerases (chemistry)</term>
<term>Aldose-Ketose Isomerases (genetics)</term>
<term>Aldose-Ketose Isomerases (metabolism)</term>
<term>Amino Acid Sequence</term>
<term>Calcium (metabolism)</term>
<term>Cobalt (metabolism)</term>
<term>Enzyme Stability</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Mutation</term>
<term>Sequence Alignment</term>
<term>Streptomyces (enzymology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Aldose-ketose isomerases ()</term>
<term>Aldose-ketose isomerases (génétique)</term>
<term>Aldose-ketose isomerases (métabolisme)</term>
<term>Alignement de séquences</term>
<term>Calcium (métabolisme)</term>
<term>Cinétique</term>
<term>Cobalt (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Mutation</term>
<term>Stabilité enzymatique</term>
<term>Streptomyces (enzymologie)</term>
<term>Séquence d'acides aminés</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aldose-Ketose Isomerases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aldose-Ketose Isomerases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aldose-Ketose Isomerases</term>
<term>Calcium</term>
<term>Cobalt</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Streptomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Streptomyces</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aldose-ketose isomerases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aldose-ketose isomerases</term>
<term>Calcium</term>
<term>Cobalt</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Enzyme Stability</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Mutation</term>
<term>Sequence Alignment</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Aldose-ketose isomerases</term>
<term>Alignement de séquences</term>
<term>Cinétique</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Mutation</term>
<term>Stabilité enzymatique</term>
<term>Séquence d'acides aminés</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The role of two amino acid residues linked to the two catalytic histidines His54 and His220 in kinetics and physicochemical properties of the Streptomyces sp. SK glucose isomerase (SKGI) was investigated by site-directed mutagenesis and molecular modeling. Two single mutations, F53L and G219D, and a double mutation F53L/G219D was introduced into the xylA SKGI gene. The F53L mutation increases the thermostability and the catalytic efficiency and also slightly shifts the optimum pH from 6.5 to 7, but displays a profile being similar to that of the wild-type enzyme concerning the effect of various metal ions. The G219D mutant is resistant to calcium inhibition retaining about 80% of its residual activity in 10 mM Ca²⁺ instead of 10% for the wild-type. This variant is activated by Mn²⁺ ions, but not Co²⁺, as seen for the wild-type enzyme. It does not require the latter for its thermostability, but has its half-life time displaced from 50 to 20 min at 85°C. The double mutation F53L/G219D restores the thermostability as seen for the wild-type enzyme while maintaining the resistance to the calcium inhibition. Molecular modeling suggests that the increase in thermostability is due to new hydrophobic interactions stabilizing α2 helix and that the resistance to calcium inhibition is a result of narrowing the binding site of catalytic ion.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22139345</PMID>
<DateCreated><Year>2012</Year>
<Month>3</Month>
<Day>22</Day>
</DateCreated>
<DateCompleted><Year>2012</Year>
<Month>08</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1476-5535</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>39</Volume>
<Issue>4</Issue>
<PubDate><Year>2012</Year>
<Month>Apr</Month>
</PubDate>
</JournalIssue>
<Title>Journal of industrial microbiology & biotechnology</Title>
<ISOAbbreviation>J. Ind. Microbiol. Biotechnol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.</ArticleTitle>
<Pagination><MedlinePgn>537-46</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1007/s10295-011-1061-1</ELocationID>
<Abstract><AbstractText>The role of two amino acid residues linked to the two catalytic histidines His54 and His220 in kinetics and physicochemical properties of the Streptomyces sp. SK glucose isomerase (SKGI) was investigated by site-directed mutagenesis and molecular modeling. Two single mutations, F53L and G219D, and a double mutation F53L/G219D was introduced into the xylA SKGI gene. The F53L mutation increases the thermostability and the catalytic efficiency and also slightly shifts the optimum pH from 6.5 to 7, but displays a profile being similar to that of the wild-type enzyme concerning the effect of various metal ions. The G219D mutant is resistant to calcium inhibition retaining about 80% of its residual activity in 10 mM Ca²⁺ instead of 10% for the wild-type. This variant is activated by Mn²⁺ ions, but not Co²⁺, as seen for the wild-type enzyme. It does not require the latter for its thermostability, but has its half-life time displaced from 50 to 20 min at 85°C. The double mutation F53L/G219D restores the thermostability as seen for the wild-type enzyme while maintaining the resistance to the calcium inhibition. Molecular modeling suggests that the increase in thermostability is due to new hydrophobic interactions stabilizing α2 helix and that the resistance to calcium inhibition is a result of narrowing the binding site of catalytic ion.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hlima</LastName>
<ForeName>Hajer Ben</ForeName>
<Initials>HB</Initials>
<AffiliationInfo><Affiliation>Laboratoire de Microorganismes et de Biomolécules, Centre de Biotechnologie de Sfax, Université de Sfax, Route de Sidi Mansour Km 6, B.P 1177, 3018 Sfax, Tunisia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Aghajari</LastName>
<ForeName>Nushin</ForeName>
<Initials>N</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ali</LastName>
<ForeName>Mamdouh Ben</ForeName>
<Initials>MB</Initials>
</Author>
<Author ValidYN="Y"><LastName>Haser</LastName>
<ForeName>Richard</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Bejar</LastName>
<ForeName>Samir</ForeName>
<Initials>S</Initials>
</Author>
</AuthorList>
<Language>ENG</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2011</Year>
<Month>Dec</Month>
<Day>04</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>J Ind Microbiol Biotechnol</MedlineTA>
<NlmUniqueID>9705544</NlmUniqueID>
<ISSNLinking>1367-5435</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>3G0H8C9362</RegistryNumber>
<NameOfSubstance UI="D003035">Cobalt</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 5.3.1.-</RegistryNumber>
<NameOfSubstance UI="D019747">Aldose-Ketose Isomerases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 5.3.1.5</RegistryNumber>
<NameOfSubstance UI="C023298">xylose isomerase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber>
<NameOfSubstance UI="D002118">Calcium</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D019747" MajorTopicYN="N">Aldose-Ketose Isomerases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003035" MajorTopicYN="N">Cobalt</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016297" MajorTopicYN="Y">Mutagenesis, Site-Directed</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013302" MajorTopicYN="N">Streptomyces</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year>
<Month>9</Month>
<Day>9</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2011</Year>
<Month>11</Month>
<Day>8</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2011</Year>
<Month>12</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2011</Year>
<Month>12</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2012</Year>
<Month>8</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">22139345</ArticleId>
<ArticleId IdType="doi">10.1007/s10295-011-1061-1</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Tunisie</li>
</country>
</list>
<tree><noCountry><name sortKey="Aghajari, Nushin" sort="Aghajari, Nushin" uniqKey="Aghajari N" first="Nushin" last="Aghajari">Nushin Aghajari</name>
<name sortKey="Ali, Mamdouh Ben" sort="Ali, Mamdouh Ben" uniqKey="Ali M" first="Mamdouh Ben" last="Ali">Mamdouh Ben Ali</name>
<name sortKey="Bejar, Samir" sort="Bejar, Samir" uniqKey="Bejar S" first="Samir" last="Bejar">Samir Bejar</name>
<name sortKey="Haser, Richard" sort="Haser, Richard" uniqKey="Haser R" first="Richard" last="Haser">Richard Haser</name>
</noCountry>
<country name="Tunisie"><noRegion><name sortKey="Hlima, Hajer Ben" sort="Hlima, Hajer Ben" uniqKey="Hlima H" first="Hajer Ben" last="Hlima">Hajer Ben Hlima</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Terre/explor/CobaltMaghrebV1/Data/PubMed/Checkpoint

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000041 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 000041 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Terre
   |area=    CobaltMaghrebV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:22139345
   |texte=   Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i   -Sk "pubmed:22139345" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a CobaltMaghrebV1

This area was generated with Dilib version V0.6.32.
Data generation: Tue Nov 14 12:56:51 2017. Site generation: Mon Feb 12 07:59:49 2024

	Serveur d'exploration sur le cobalt au Maghreb
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur le cobalt au Maghreb

Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.

Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca²⁺ inhibition and Co²⁺ independent.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki