N-acetylneuraminate epimerase

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N-acetylneuraminate epimerase
Identifiers
EC no. 5.1.3.24
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N-acetylneuraminate epimerase (EC 5.1.3.24, sialic acid epimerase, N-acetylneuraminate mutarotase, sialic acid mutarotase, YjhT, NanM) is an enzyme with systematic name N-acetyl-alpha-neuraminate 2-epimerase. [1] This enzyme catalyses the following chemical reaction

Contents

N-acetyl-alpha-neuraminate N-acetyl-beta-neuraminate

Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages.

See also

Related Research Articles

<span class="mw-page-title-main">Sialic acid</span> Class of chemical compounds

Sialic acids are a class of alpha-keto acid sugars with a nine-carbon backbone. The term "sialic acid" was first introduced by Swedish biochemist Gunnar Blix in 1952. The most common member of this group is N-acetylneuraminic acid found in animals and some prokaryotes.

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

Sialyltransferases are enzymes that transfer sialic acid to nascent oligosaccharide. Each sialyltransferase is specific for a particular sugar substrate. Sialyltransferases add sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins.

<i>N</i>-Acetylmannosamine Chemical compound

N-Acetylmannosamine is a hexosamine monosaccharide. It is a neutral, stable naturally occurring compound. N-Acetylmannosamine is also known as N-Acetyl-D-mannosamine monohydrate,, N-Acetyl-D-mannosamine which can be abbreviated to ManNAc or, less commonly, NAM). ManNAc is the first committed biological precursor of N-acetylneuraminic acid. Sialic acids are the negatively charged, terminal monosaccharides of carbohydrate chains that are attached to glycoproteins and glycolipids (glycans).

In enzymology, an aldose 1-epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">N-acetylneuraminate lyase</span>

The enzyme N-acetylneuraminate lyase catalyzes the chemical reaction

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

<span class="mw-page-title-main">N-acetylneuraminate synthase</span>

In enzymology, a N-acetylneuraminate synthase (EC 2.5.1.56) is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-galactoside alpha-2,3-sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a beta-galactoside alpha-2,6-sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a lactosylceramide alpha-2,3-sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a lactosylceramide alpha-2,6-N-sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a monosialoganglioside sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a N-acetyllactosaminide alpha-2,3-sialyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a neolactotetraosylceramide alpha-2,3-sialyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">GNE (gene)</span> Protein-coding gene in humans

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is an enzyme that in humans is encoded by the GNE gene.

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

The Kelch motif is a region of protein sequence found widely in proteins from bacteria and eukaryotes. This sequence motif is composed of about 50 amino acid residues which form a structure of a four stranded beta-sheet "blade". This sequence motif is found in between five and eight tandem copies per protein which fold together to form a larger circular solenoid structure called a beta-propeller domain.

(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:1-O-(O- - -O-beta-D-galactopyranosyl- -beta-D-glucopyranosyl)-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction

Alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide 6-alpha-sialyltransferase is an enzyme with systematic name CMP-N-acetylneuraminate:N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)- N-acetyl-D-galactosaminide galactosamine-6-alpha-N-acetylneuraminyltransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine 2-epimerase (hydrolysing) (EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase, GNE (gene), siaA (gene), neuC (gene)) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine hydrolase (2-epimerising). 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. Severi E, Müller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH (February 2008). "Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT". The Journal of Biological Chemistry. 283 (8): 4841–9. doi: 10.1074/jbc.M707822200 . PMID   18063573.