Based on the residues in the active site what family of proteases does pepsin belong to?
singleAnswer
Aspartic protease
Pepsin
Based on the residues in the active site what family of proteases does pepsin belong to?
Pepsin Aspartic protease Protease HIV-1 protease Serine protease Catalytic triad Papain Glutamic protease Scytalidopepsin B Yapsin 1
<b>Pepsin</b> is an endopeptidase that breaks down proteins into smaller amino acids. 
It is produced ... <b>Pepsin</b> is an aspartic <b>protease</b>, using a catalytic aspartate in its 
<b>active site</b>. ... An acidic substance that was able to convert nitrogen-<b>based</b> foods 
into ... for hydrophobic, preferably aromatic, <b>residues</b> in P1 and P1&#39; positions. Aspartic <b>proteases</b> are a catalytic type of <b>protease</b> enzymes that use an activated 
water molecule bound to one or more aspartate <b>residues</b> for catalysis of their 
peptide substrates. In general, they have two highly conserved aspartates in the 
<b>active site</b> and ... Aspartyl <b>proteases</b> are a highly specific <b>family of proteases</b> – 
they tend to&nbsp;... A <b>protease</b> is an enzyme that catalyzes (increases the rate of) proteolysis, the 
breakdown of proteins into smaller polypeptides or single amino acids. They <b>do</b> 
this by cleaving the peptide bonds within proteins by hydrolysis, ... Within each &#39;
clan&#39;, <b>proteases</b> are classified into <b>families based</b> on sequence similarity (e.g. the 
S1&nbsp;... HIV-1 <b>protease</b> (PR) is a retroviral aspartyl <b>protease</b> (<b>retropepsin</b>), an enzyme 
involved with peptide bond hydrolysis in retroviruses, that is essential for the&nbsp;... Serine <b>proteases</b> (or serine endopeptidases) are enzymes that cleave peptide 
bonds in proteins, in which serine serves as the nucleophilic amino acid at the (
enzyme&#39;s) <b>active site</b>. They are found ubiquitously in both eukaryotes and 
prokaryotes. Serine <b>proteases</b> fall into two broad categories <b>based</b> on their 
structure: ... The majority <b>belong to</b> the S1 <b>family</b> of the PA clan (superfamily) of 
<b>proteases</b>. A catalytic triad is a set of three coordinated amino acids that can be found in the 
<b>active site</b> of ... Triads are an inter-dependent set of <b>residues in the active site</b> of 
an enzyme and act in concert with ... For example, papain uses asparagine as its 
third triad member which orients the histidine <b>base</b> but <b>does</b> not act as an acid. Papain, also known as papaya proteinase I, is a cysteine <b>protease</b> (EC 3.4.22.2) 
enzyme ... Papain <b>belongs to</b> a <b>family</b> of related proteins with a wide variety of 
activities, including ... Amino acid <b>residues</b> within the pro-region mediate their 
membrane ... This cleft contains the <b>active site</b>, which contains a catalytic diad 
that has&nbsp;... Glutamic <b>proteases</b> are a <b>group of proteolytic</b> enzymes containing a glutamic acid 
<b>residue</b> within the <b>active site</b>. ... <b>protease</b>, but structural determination showed it 
to <b>belong to</b> a novel <b>protease family</b>. ... produces non Streptomyces <b>pepsin</b> 
inhibitor and N-diazoacetyl-DL-norleucine methylester sensitive acid <b>proteases</b>&quot;. Scytalidocarboxyl peptidase B, also known as Scytalidoglutamic peptidase and ... 
The <b>active</b>-<b>site residues</b>, glutamic acid (E) and glutamine (Q), was used to coin 
the name of the <b>family of proteases</b>, eqolisins, to which Scytalidoglutamic 
peptidase B <b>belongs</b>. This enzyme catalyses the following chemical reaction &middot; 
Hydrolysis&nbsp;... Yapsin 1 is an enzyme. This enzyme catalyses the following chemical reaction &middot; 
Hydrolyses ... This enzyme <b>belongs to</b> the peptidase <b>family</b> A1 of <b>pepsin</b>. ... of 
various prohormone mono- and paired-basic <b>residue</b> sites by yeast aspartic 
<b>protease</b> 3&quot;. ... <b>residues</b> flanking the P1 site: correlation with electronegative 
<b>active</b>-<b>site</b>&nbsp;...
Acid proteases
Protease