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Found in plants, bacteria, and yeast, cystathionine beta-lyase is an essential part of the methionine biosynthesis pathway as homocysteine can be directly converted into methionine by methionine synthase.
The CHAP domain is found in a wide range of protein architectures; it is commonly associated with bacterial type SH3 domains and with several families of amidase domains. It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack mechanism. [1] [2]
Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile. [1] The human genome encodes eleven cysteine cathepsins which have a broad range of physiological functions. [3] In some parasites papain-like proteases have roles in host invasion, such as cruzipain from ...
The cysteine sulfhydryl group is nucleophilic and easily oxidized. The reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pK a values close to neutrality, so are often in their reactive thiolate form in the cell. [23] Because of its high reactivity, the sulfhydryl group of cysteine has numerous biological ...
Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, the latex of dozens of different plant families are known to contain cysteine proteases. [2] Cysteine proteases are used as an ingredient in meat tenderizers.
Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. [4] [5] [6] This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import and assembly (Mia40), which has 2 ...
The two thioether linkages are typically made by cysteine residues of the protein. These linkages do not allow the heme C to easily dissociate from the holoprotein , cytochrome c , compared with the more easily dissociated heme B that may dissociate from the holoprotein, the heme-protein complex, even under mild conditions.
D. melanogaster and D. discoides have truncated N-terminal extensions and therefore prevent the conserved histidine and cysteine heme ligand residues. However, the Anopheles gambiae sequence has a longer N-terminal extension than the human enzyme and contains the conserved histidine and cysteine heme ligand residues like the human heme.