Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis.

doi:10.1128/jb.176.23.7161-7168.1994

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Article

Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis.

Journal of bacteriology - 1 Dec 1994

Welsh K M, Trach K A, Folger C, Hoch J A

Abstract excerpt

An essential guanine nucleotide-binding protein, Obg, of Bacillus subtilis has been characterized with respect to its enzymatic activity for GTP. The protein was seen to hydrolyze GTP with a Km of 5.4 microM and a kcat of 0.0061 min-1 at 37 degrees C. GDP was a competitive inhibitor of this hydrolysis, with an inhibition constant of 1.7 microM at 37 degrees C. The dissociation constant for GDP from the Obg...

Topics

Bacillus subtilis
Bacterial Proteins
GTP Phosphohydrolases
GTP-Binding Proteins
Genes, Bacterial
Genes, Lethal
Guanosine Diphosphate
Guanosine Triphosphate
Hot Temperature
Hydrolysis
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Biological

Molecular Weight

Mutation

Phosphates

Phosphoproteins

Phosphorylation

Source

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Identifiers

PMID: 7961487
DOI: 10.1128/jb.176.23.7161-7168.1994
PMCID: PMC197103

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7961487-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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