The urea cycle of Helicobacter pylori

Article Abstract:

Helicobacter pylori is a Gram-negative bacteria that attaches and grows in the upper gastrointestinal tract where it causes active chronic gastritis. It has been suggested that this bacteria is able to excrete nitrogen by formation of metabolites from amino acids via deamination. NMR spectroscopy and radioactive tracer analysis reveal that nitrogen excretion in H. pylori occurs through a urea cycle and not through deamination reactions as previously thought. Argininosuccinate synthetase and argininosuccinase are the enzymes involved in the urea cycle.

Microbial metabolism, Urea

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Acetyl-CoA carboxylase activity in Helicobacter pylori and the requirement of increased CO2 for growth

Article Abstract:

The acetyl-CoA carboxylase of Helicobacter pylori carboxylates acetyl-CoA to form malonyl-CoA in the presence of high levels of bicarbonate. The enzyme is a multiprotein complex containing biotin and has a molecular mass of 235 kDa. The enzymatic activity requires acetyl-CoA and is suppressible by avidin. However, the carboxylase activity is unaltered by avidin treated with biotin. The enzyme has a somewhat low affinity for bicarbonates. The formation of malonyl-CoA forms more slowly than the usage of acetyl-CoA.

Research, Carbon dioxide, Microbial enzymes

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Catalase (KatA) and KatA-associated protein (KapA) are essential to persistent colonization in the Helicobacter pylori SS1 mouse model

Article Abstract:

Results indicate that neither catalase or its associated protein are required for infection and initial colonization of Helicobacter pylori SS1. However, to sustain long-term infection and colonization H. pylori SS1 requires the proteins as shown by the inability of the mutants to establish colonization over a 24-week period.

United Kingdom, Australia, Bacterial infections, Protein metabolism, Enzyme synthesis

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