Related Research Articles
Histone methyltransferases (HMT) are histone-modifying enzymes, that catalyze the transfer of one, two, or three methyl groups to lysine and arginine residues of histone proteins. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4. Two major types of histone methyltranferases exist, lysine-specific and arginine-specific. In both types of histone methyltransferases, S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.
The genomic DNA of eukaryotes associates with histones to form chromatin. The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones. Histone methylation is a principal epigenetic modification of chromatin that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.
A carboxypeptidase is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation. At least two mechanisms have been discussed.
Kallidin is a bioactive kinin formed in response to injury from kininogen precursors through the action of kallikreins.
Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).
Dipeptidases are enzymes secreted by enterocytes into the small intestine. Dipeptidases hydrolyze bound pairs of amino acids, called dipeptides.
Carboxypeptidase B is a carboxypeptidase that preferentially acts upon basic amino acids, such as arginine and lysine. This serum enzyme is also responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid.
Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene.
Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the porcine kidney cortex. It exists as a disulfide-linked homodimer that is glygosylphosphatidylinositol (GPI)-anchored to the renal brush border of the kidney. The active site on each homodimer is made up of a barrel subunit with binuclear zinc ions that are bridged by the Gly125 side-chain located at the bottom of the barrel.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-methyl-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Met-Xaa dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Membrane dipeptidase (EC 3.4.13.19, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase, nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MBD, MDP, leukotriene D4 hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction
Beta-Ala-His dipeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Dipeptidase E is an enzyme. This enzyme catalyses the following chemical reaction
C-terminal processing peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Peptidyl-Lys metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Nardilysin is an enzyme. This enzyme catalyses the following chemical reaction
References
- ↑ Kumon A, Matsuoka Y, Kakimoto Y, Nakajima T, Sano I (March 1970). "A peptidase that hydrolyzes Na-(gamma-aminobutyryl)lysine". Biochimica et Biophysica Acta (BBA) - Protein Structure. 200 (3): 466–74. doi:10.1016/0005-2795(70)90103-0. PMID 5436646.
