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Publisher : published by portland press on behalf of the biochemical society

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Academic Journal

The iron-type nitrile hydratase activator protein is a GTPase.

Authors : Gumataotao N; Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 W Sheridan Rd, Chicago, IL 60660, U.S.A.; Lankathilaka KP

Subjects: Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*chemistry ; GTP Phosphohydrolases/GTP Phosphohydrolases/GTP Phosphohydrolases/*chemistry ; Guanosine Triphosphate/Guanosine Triphosphate/Guanosine Triphosphate/*chemistry

Source: The Biochemical journal [Biochem J] 2017 Jan 15; Vol. 474 (2), pp. 247-258. Date of Electronic Publication: 2016 Nov 02.Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R

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Mechanistic insight into the reaction catalysed by bacterial type II dehydroquinases.

Authors : Coderch C; Departamento de Ciencias Biomédicas, Universidad de Alcalá, 28871 Alcalá de Henares, Madrid, Spain.; Lence E

Subjects: Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*chemistry ; Helicobacter pylori/Helicobacter pylori/Helicobacter pylori/*enzymology ; Hydro-Lyases/Hydro-Lyases/Hydro-Lyases/*chemistry

Source: The Biochemical journal [Biochem J] 2014 Mar 15; Vol. 458 (3), pp. 547-57.Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R

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Insights into substrate binding and catalysis in bacterial type I dehydroquinase.

Authors : Maneiro M; Centro Singular de Investigación en Química Biológica y Materiales Moleculares (CIQUS), Universidad de Santiago de Compostela, calle Jenaro de la Fuente s/n, 15782 Santiago de Compostela, Spain.; Peón A

Subjects: Hydro-Lyases/Hydro-Lyases/Hydro-Lyases/*metabolism; Amino Acid Sequence ; Catalysis

Source: The Biochemical journal [Biochem J] 2014 Sep 15; Vol. 462 (3), pp. 415-24.Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R

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The chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal.

Authors : Cronan JE; Departments of Microbiology and Biochemistry University of Illinois, Urbana, IL 61801, U.S.A.

Subjects: Acyl Carrier Protein/Acyl Carrier Protein/Acyl Carrier Protein/*metabolism ; Pantetheine/Pantetheine/Pantetheine/*analogs & derivatives; Acyl Carrier Protein/Acyl Carrier Protein/Acyl Carrier Protein/chemistry

Source: The Biochemical journal [Biochem J] 2014 Jun 01; Vol. 460 (2), pp. 157-63.Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R

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