Acrocylindropepsin

Last updated
Acrocylindropepsin
Identifiers
EC no. 3.4.23.28
CAS no. 37288-84-9
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

Acrocylindropepsin (EC 3.4.23.28, Acrocylindrium proteinase, Acrocylindrium acid proteinase) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction

Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-Cys(SO3H), Glu21-Arg and Asn3-Gln, although not Gln4-His

This enzyme is present in fungus Acrocylindrium sp.

Related Research Articles

Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction

In enzymology, a (S)-2-haloacid dehalogenase (EC 3.8.1.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a glutamate—ethylamine ligase (EC 6.3.1.6) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Proteinase K</span> Broad-spectrum serine protease

In molecular biology, Proteinase K is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Parengyodontium album. Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons.

The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction

In enzymology, a guanidinobutyrase (EC 3.5.3.7) is an enzyme that catalyzes the chemical reaction

In enzymology, an adenosylmethionine-8-amino-7-oxononanoate transaminase is an enzyme that catalyzes the chemical reaction

Cucumisin is an enzyme. This enzyme catalyzes hydrolysis of a wide range of proteins. It has been identified as an allergen in humans.

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

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

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

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

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

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

Scytalidopepsin A (EC 3.4.23.31, Scytalidium aspartic proteinase A, Scytalidium lignicolum aspartic proteinase, Scytalidium lignicolum aspartic proteinase A-2, Scytalidium lignicolum aspartic proteinase A-I, Scytalidium lignicolum aspartic proteinase C, Scytalidium lignicolum carboxyl proteinase, Scytalidium lignicolum acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction

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

Scytalidocarboxyl peptidase B, also known as Scytalidoglutamic peptidase and Scytalidopepsin B is a proteolytic enzyme. It was previously thought to be an aspartic protease, but determination of its molecular structure showed it to belong a novel group of proteases, glutamic protease.

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

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

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

Glutamic proteases are a group of proteolytic enzymes containing a glutamic acid residue within the active site. This type of protease was first described in 2004 and became the sixth catalytic type of protease. Members of this group of protease had been previously assumed to be an aspartate protease, but structural determination showed it to belong to a novel protease family. The first structure of this group of protease was scytalidoglutamic peptidase, the active site of which contains a catalytic dyad, glutamic acid (E) and glutamine (Q), which give rise to the name eqolisin. This group of proteases are found primarily in pathogenic fungi affecting plant and human.

<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. Uchino F, Kurono Y, Doi S (1967). "Purification and some properties of crystalline acid protease from Acrocylindrium sp". Agric. Biol. Chem. 31: 428–434. doi: 10.1271/bbb1961.31.428 .
  2. Ichihara S, Uchino F (1975). "The specificity of acid proteinase from Acrocylindrium". Agric. Biol. Chem. 39: 423–428. doi: 10.1271/bbb1961.39.423 .
  3. Takahashi K, Chang WJ (September 1976). "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin". Journal of Biochemistry. 80 (3): 497–506. PMID   10290.