Chondroitin ABC lyase

Last updated
chondroitin-sulfate-ABC endolyase
Identifiers
EC no. 4.2.2.20
CAS no. 9024-13-9
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
chondroitin-sulfate-ABC exolyase
Identifiers
EC no. 4.2.2.21
CAS no. 9024-13-9
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

Chondroitin ABC lyase (EC 4.2.2.20 EC 4.2.2.21, chondroitinase, chondroitin ABC eliminase, chondroitinase ABC) is an enzyme with systematic name chondroitin ABC lyase. [1] [2] This enzyme catalyses the following chemical reaction

Contents

Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups

This enzyme acts on chondroitin 4-sulfate, chondroitin 6-sulfate and dermatan sulfate.

Uses

Following a spinal cord injury, this enzyme can be used to erode scar tissue that can interfere with regeneration. [3]

Related Research Articles

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

Heparin, also known as unfractionated heparin (UFH), is a medication and naturally occurring glycosaminoglycan. Since heparins depend on the activity of antithrombin, they are considered anticoagulants. Specifically it is also used in the treatment of heart attacks and unstable angina. It is given intravenously or by injection under the skin. Other uses for its anticoagulant properties include inside blood specimen test tubes and kidney dialysis machines.

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

Beta-hexosaminidase subunit beta is an enzyme that in humans is encoded by the HEXB gene.

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

Steroid sulfatase (STS), or steryl-sulfatase, formerly known as arylsulfatase C, is a sulfatase enzyme involved in the metabolism of steroids. It is encoded by the STS gene.

Chondroitinase treatment is a treatment of proteoglycans, a protein in the fluid among cells where they affect neural activity. Chondroitinase treatment has been shown to allow adults vision to be restored as far as ocular dominance is concerned. Moreover, there is some evidence that Chondroitinase could be used for the treatment of spinal injuries.

<span class="mw-page-title-main">Glial scar</span> Mass formed in response to injury to the nervous system

A glial scar formation (gliosis) is a reactive cellular process involving astrogliosis that occurs after injury to the central nervous system. As with scarring in other organs and tissues, the glial scar is the body's mechanism to protect and begin the healing process in the nervous system.

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

The enzyme ornithine cyclodeaminase catalyzes the chemical reaction

<span class="mw-page-title-main">Phenylalanine ammonia-lyase</span>

The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:

<span class="mw-page-title-main">3-mercaptopyruvate sulfurtransferase</span> Class of enzymes

In enzymology, a 3-mercaptopyruvate sulfurtransferase is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.

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

Hexosaminidase A (alpha polypeptide), also known as HEXA, is an enzyme that in humans is encoded by the HEXA gene, located on the 15th chromosome.

The enzyme chondroitin AC lyase catalyzes the chemical reaction

The enzyme chondroitin B lyase catalyzes the following process:

The enzyme chondroitin-sulfate-ABC endolyase catalyzes the following process:

The enzyme chondroitin-sulfate-ABC exolyase catalyzes the following process:

The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction

The enzyme chondro-6-sulfatase (EC 3.1.6.10) catalyzes the reaction

Phosphatidate cytidylyltransferase (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.

<span class="mw-page-title-main">Xylosyltransferase</span> Class of enzymes

Xylosyltransferase are transferase enzymes which act upon xylose and are classified under EC 2.4.2.

Glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:D-glucuronyl-(1->3)-beta-D-galactosyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction

Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Dihydrodipicolinate synthase</span> Class of enzymes

4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction

References

  1. Yamagata T, Saito H, Habuchi O, Suzuki S (April 1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". The Journal of Biological Chemistry. 243 (7): 1523–35. doi: 10.1016/S0021-9258(18)93574-X . PMID   5647268.
  2. Saito H, Yamagata T, Suzuki S (April 1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". The Journal of Biological Chemistry. 243 (7): 1536–42. doi: 10.1016/S0021-9258(18)93575-1 . PMID   4231029.
  3. Bartus K, James ND, Didangelos A, Bosch KD, Verhaagen J, Yáñez-Muñoz RJ, Rogers JH, Schneider BL, Muir EM, Bradbury EJ (April 2014). "Large-scale chondroitin sulfate proteoglycan digestion with chondroitinase gene therapy leads to reduced pathology and modulates macrophage phenotype following spinal cord contusion injury". The Journal of Neuroscience. 34 (14): 4822–36. doi:10.1523/JNEUROSCI.4369-13.2014. PMC   3972714 . PMID   24695702.