Cephalosporin-C deacetylase

Last updated
cephalosporin-C deacetylase
Identifiers
EC no. 3.1.1.41
CAS no. 52227-71-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

The enzyme cephalosporin-C deacetylase (EC 3.1.1.41) catalyzes the reaction

cephalosporin C + H2O deacetylcephalosporin C + acetate

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cephalosporin-C acetylhydrolase. Other names in common use include cephalosporin C acetyl-hydrolase, cephalosporin C acetylase, cephalosporin acetylesterase, cephalosporin C acetylesterase, cephalosporin C acetyl-esterase, and cephalosporin C deacetylase. This enzyme participates in penicillin and cephalosporin biosynthesis.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1L7A, 1ODS, 1ODT, and 1VLQ.

Related Research Articles

Thioesterases are enzymes which belong to the esterase family. Esterases, in turn, are one type of the several hydrolases known.

The enzyme 6-acetylglucose deacetylase (EC 3.1.1.33) catalyzes the reaction

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The enzyme N-acetylgalactosaminoglycan deacetylase (EC 3.1.1.58) catalyzes the reaction

The enzyme sialate O-acetylesterase (EC 3.1.1.53) catalyzes the reaction

In enzymology, an acetylornithine deacetylase (EC 3.5.1.16) is an enzyme that catalyzes the chemical reaction

In enzymology, a glutaryl-7-aminocephalosporanic-acid acylase (EC 3.5.1.93) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetyl-beta-alanine deacetylase (EC 3.5.1.21) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetyldiaminopimelate deacetylase (EC 3.5.1.47) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">N-acetylglucosamine-6-phosphate deacetylase</span>

In enzymology, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25), also known as GlcNAc-6-phosphate deacetylase or NagA, is an enzyme that catalyzes the deacetylation of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to glucosamine-6-phosphate (GlcN-6-P):

In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction

In enzymology, a deacetylcephalosporin-C acetyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Homocitrate synthase</span> Enzyme

In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction

2-deoxystreptamine N-acetyl-D-glucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ribostamycin N-acetylglucosaminyltransferase. This enzyme catalyses the following chemical reaction

The enzyme Rhamnogalacturonan acetylesterase is an enzyme catalyses the reaction

N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (EC 3.5.1.103, MshB) is an enzyme with systematic name 1-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase. This enzyme catalyses the following chemical reaction

2'-N-acetylparomamine deacetylase (EC 3.5.1.112, btrD (gene), neoL (gene), kanN (gene)) is an enzyme with systematic name 2'-N-acetylparomamine hydrolase (acetate-forming). This enzyme catalyses the following chemical reaction

2'''-acetyl-6'''-hydroxyneomycin C deacetylase (EC 3.5.1.113, neoL (gene)) is an enzyme with systematic name 2'''-acetyl-6'''-hydroxyneomycin C hydrolase (acetate-forming). This enzyme catalyses the following chemical reaction

References


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