Coccolysin

Last updated
Coccolysin
Identifiers
EC no. 3.4.24.30
CAS no. 156859-08-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Coccolysin (EC 3.4.24.30, Streptococcus thermophilus intracellular proteinase, EM 19000) is an enzyme. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

Preferential cleavage: -Leu, -Phe, -Tyr, -Ala

This endopeptidase is present in S. thermophilus, S. diacetilactis and S. faecalis.

Related Research Articles

A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase.

Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Lysin</span>

Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternative mechanisms. Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's autolytic mechanisms such as autolysins.

<span class="mw-page-title-main">Glycerol dehydrogenase</span>

Glycerol dehydrogenase (EC 1.1.1.6, also known as NAD+-linked glycerol dehydrogenase, glycerol: NAD+ 2-oxidoreductase, GDH, GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD+ to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone).

In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an aspartate racemase is an enzyme that catalyzes the following chemical reaction:

Poly(3-hydroxybutyrate) depolymerase (EC 3.1.1.75, PHB depolymerase, systematic name poly[(R)-3-hydroxybutanoate] hydrolase) is an enzyme used in the degradation processes of a natural polyester poly(3-hydroxyburate). This enzyme has growing commercialization interests due to it implications in biodegradable plastic decomposition.

In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NLN (gene)</span> Protein-coding gene in the species Homo sapiens

Neurolysin, mitochondrial is a protein that in humans is encoded by the NLN gene. It is a 78-kDa enzyme, widely distributed in mammalian tissues and found in various subcellular locations that vary with cell type. Neurolysin exemplifies the ability of neuropeptidases to target various cleavage site sequences by hydrolyzing them in vitro, and metabolism of neurotensin is the most important role of neurolysin in vivo. Neurolysin has also been implicated in pain control, blood pressure regulation, sepsis, reproduction, cancer biology pathogenesis of stroke, and glucose metabolism.

<span class="mw-page-title-main">Ecadotril</span> Chemical compound

Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC 3.4.24.11) and determined by the presence of peptidase family M13 as a neutral endopeptidase inhibited by phosphoramidon. Ecadotril is the (S)-enantiomer of racecadotril. NEP-like enzymes include the endothelin-converting enzymes. The peptidase M13 family believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides, neprilysin is another member of this group, in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water molecule. The peptidase domain for members of this family also contains a bacterial member and resembles that of thermolysin the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH. Thermolysin complexed with the inhibitor (S)-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase").

<span class="mw-page-title-main">Oligopeptidase</span> Enzymes that cleaves peptides but not proteins

An Oligopeptidase is an enzyme that cleaves peptides but not proteins. This property is due to its structure: the active site of this enzyme is located at the end of a narrow cavity which can only be reached by peptides.

Bacterial leucyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Glutamyl endopeptidase II is an enzyme. This enzyme catalyses the following chemical reaction

Mycolysin is an enzyme. This enzyme catalyses the following chemical reaction

Peptidyl-Asp metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction

Deuterolysin is an enzyme. This enzyme catalyses the following chemical reaction

Ophiolysin is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction

Mucrolysin is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Sedolisin</span>

The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.

References

  1. Desmazeaud MJ (1974). "[General properties and specificity of action of a neutral intracellular endopeptidase from Streptococcus thermophilus]". Biochimie. 56 (9): 1173–1181. doi:10.1016/s0300-9084(74)80008-8. PMID   4451671.
  2. Desmazeaud MJ, Zevaco C (1976). "General properties and substrate specificity of an intracellular neutral protease from Streptococcus diaceti lactis" (PDF). Annales de Biologie Animale, Biochimie, et Biophysique. 16 (6): 851–868. doi: 10.1051/rnd:19760608 .
  3. Smith RA, Green J, Kopper PH (July 1980). "The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis". Archives of Biochemistry and Biophysics. 202 (2): 629–638. doi:10.1016/0003-9861(80)90471-3. PMID   6779709.
  4. Mäkinen PL, Clewell DB, An F, Mäkinen KK (February 1989). "Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10)". The Journal of Biological Chemistry. 264 (6): 3325–3334. doi: 10.1016/S0021-9258(18)94069-X . PMID   2536744.