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Several enzymes present in mammalian systems are now recognized as having the same conserved catalytic domain, including the eEF-2 kinases [ 19 ] [ 20 ] and TRP-PLIK, a bifunctional protein with kinase and ion channel activities [ 21 ] .

CEES is a monofunctional analog of sulfur mustard (bis-2-(chloroethyl)sulfide) which a bifunctional vesicant and a chemical warfare agent.

Metazoans and plants have a two-component capping system consisting of a bifunctional triphosphatase-guanylyltransferase polypeptide and a separate methyltransferase polypeptide, whereas fungi contain a three-component system consisting of separate triphosphatase, guanylyltransferase, and methyltransferase gene products.

Rabbit anti-PKA RI?

was prepared by synthesizing the N-terminal 18 residues of human RI?

protein and conjugating this peptide (MESGSTAASEEARSLREC) to keyhole limpet haemocyanin (KLH) via the bifunctional reagent, m-maleimidobenzoyl-N-hydroxysuccinimide ester (MES).

I have demonstrated that a gene coding for a bifunctional catalase-peroxidase is likely a transfer from archaea to a variety of pathogenic bacteria, including E.

These same organisms also possess AroQ•PheA bifunctional proteins whose AroQ domains also form a cohesive homology grouping.

Examples are the bifunctional proteins ThrA (aspartokinase I and homoserine dehydrogenase I) and MetL (aspartokinase II and homoserine dehydrogenase II) where only the amino-terminal modules representing the kinase activities have been identified on the basis of their sequence similarity to the E.

When two paralogs of such a bifunctional gene are produced by duplication, each may be driven by positive selection to specialize in one of these functions, which it performs more efficiently than the ancestor gene, leading to the creation of two indispensable genes with distinct functions [ 11].

GSPS is a bifunctional enzyme: its synthase domain carries out the ATP-dependent fusion of two glutathione moieties to the polyamine spermidine to form the antioxidant metabolite GSP, while its amidase domain hydrolyzes the amide linkage to release glutathione and spermidine [ 26, 55, 56].

elegans , two genes each encode unusual bifunctional enzymes containing both isocitrate lyase and malate synthase domains [ 49 ] .

elegans bifunctional enzyme and none of the Meloidogyne EST reads stretches across both domains, further sequencing of the 3' end of cDNA clones from the M.

javanica isocitrate lyase ESTs will be necessary to determine whether the Meloidogyne genus contains a bifunctional glyoxylate enzyme homolog similar to that of C.


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