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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]
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.
Cysteine has l chirality in the older d / l notation based on homology to d - and l-glyceraldehyde. In the newer R / S system of designating chirality, based on the atomic numbers of atoms near the asymmetric carbon, cysteine (and selenocysteine) have R chirality, because of the presence of sulfur (or selenium) as a second neighbor to the ...
Glutamate racemase is known to use its active site to undergo racemization and participate in the cell wall biosynthesis pathway of bacteria. [2] Based on homology to other racemases and epimerases, glutamate racemase is thought to employ two active site cysteine residues as acid/base catalysts. [7]
Prxs were historically divided into three (mechanistic) classes: Typical 2-Cys Prxs; Atypical 2-Cys Prxs and; 1-Cys Prxs. The designation of "1-Cys" and "2-Cys" Prxs was introduced in 1994 [2] as it was noticed that, among the 22 Prx sequences known at the time, only one Cys residue was absolutely conserved; this is the residue now recognized as the (required) peroxidatic cysteine, C P.
Bacterial-type ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including four cysteine residues that bind to a [Fe 4 S 4] cluster. In Pyrococcus furiosus Fe 4 S 4 ferredoxin, one of the conserved Cys residues is substituted with aspartic acid.
The N-terminal glucosyltransferase catalytic domain includes amino acid residues 1–544 while the cysteine protease domain includes residues 545–801. Additionally, the translocation region incorporates amino acid residues from 802 to 1664 while the receptor binding region is part of the C-terminal region and includes amino acid residues from ...
Oxidative pathway in Gram-negative bacteria. The oxidative pathway relies, just like the isomerization pathway, on a protein relay. The first member of this protein relay is a small periplasmic protein (21 kDa) called DsbA, which has two cysteine residues that must be oxidized for it to be active.