Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

astB - succinylarginine dihydrolase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1743, JW1734, ydjT

Tocilj, A. et al., Shirai, H. et al., Schneider, B.L. et al.

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Disease relevance of astB

Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli [1].

High impact information on astB

Here we report the crystal structure of N-succinylarginine dihydrolase AstB, the second enzyme of the arginine succinyltransferase pathway, providing the first structural insight into enzymes from this pathway [1].
Disruption of astB eliminated succinylarginine dihydrolase activity and prevented arginine utilization but did not impair ornithine catabolism [2].

Associations of astB with chemical compounds

Arginine succinyltransferase and succinylarginine dihydrolase catalyze the first two steps of arginine catabolism by the arginine succinyltransferase pathway [3].

References

Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. Tocilj, A., Schrag, J.D., Li, Y., Schneider, B.L., Reitzer, L., Matte, A., Cygler, M. J. Biol. Chem. (2005) [Pubmed]
Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. Schneider, B.L., Kiupakis, A.K., Reitzer, L.J. J. Bacteriol. (1998) [Pubmed]
Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism. Shirai, H., Mizuguchi, K. FEBS Lett. (2003) [Pubmed]

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