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Gene Review:

CTSH - cathepsin H

Sus scrofa

Guncar, G. et al., Takahashi, T. et al.

Guncar, Podobnik, Pungercar, Strukelj, Turk, Turk,

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High impact information on CTSH

Cathepsin H purified from porcine spleens was studied for its specificity against various peptide and denatured protein substrates [1].
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function [2].
BACKGROUND: Cathepsin H is a lysosomal cysteine protease, involved in intracellular protein degradation [2].
CONCLUSIONS: The crystal structure of cathepsin H reveals that the mini-chain has a definitive role in substrate recognition and that carbohydrate residues attached to the body of the enzyme are involved in positioning the mini-chain in the active-site cleft [2].

References

Porcine spleen cathepsin H hydrolyzes oligopeptides solely by aminopeptidase activity. Takahashi, T., Dehdarani, A.H., Tang, J. J. Biol. Chem. (1988) [Pubmed]
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Guncar, G., Podobnik, M., Pungercar, J., Strukelj, B., Turk, V., Turk, D. Structure (1998) [Pubmed]

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