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Data · collection · 2015

Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv

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Diadenosine 5′,5′′′- P 1 , P 4 -tetraphosphate (Ap 4 A) phosphorylase from Mycobacterium tuberculosis H37Rv (MtAPA) belongs to the histidine triad motif (HIT) superfamily, but is the only member with an alanine residue at position 149 (Ala-149).

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Enzymatic analysis revealed that the Ala-149 deletion mutant displayed substrate specificity for diadenosine 5′,5′′′- P 1 , P 5 -pentaphosphate and was inactive on Ap 4 A and other substrates that are utilized by the wild-type enzyme.

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Provenance · 2 source records, 13 field assertions
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DataCite10.6084/m9.figshare.c.203729014 d agoJSON v1
DataCite10.6084/m9.figshare.c.2037290.v114 d agoJSON v1
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concepts[field].fos:biological-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:biological-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:health-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:health-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].local:field:life-sciencesmapping · DataCitevocabulary-mapper@1.0.0keywords['Biological Sciences']
concepts[field].local:field:life-sciencesmapping · DataCitevocabulary-mapper@1.0.0keywords['Biological Sciences']
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