List of EC numbers (EC 5)

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This list contains a list of EC numbers for the fifth group, EC 5, isomerases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. [1] The database is developed and maintained by Andrew McDonald. [2]

Contents

EC 5.1: Epimerases and racemases

EC 5.1.1: Acting on Amino acids and Derivatives

*No Wikipedia article

EC 5.1.2: Acting on Hydroxy acids and Derivatives

*No Wikipedia article

EC 5.1.3: Acting on Carbohydrates and Derivatives

*No Wikipedia article

EC 5.1.99: Acting on Other Compounds

*No Wikipedia article

EC 5.2: cis-trans-Isomerases

EC 5.2.1: cis-trans Isomerases (only sub-subclass identified to date)

EC 5.3: Intramolecular Oxidoreductases

EC 5.3.1: Interconverting Aldoses and Ketoses

*No Wikipedia article

EC 5.3.2: Interconverting Keto- and Enol-Groups

EC 5.3.3: Transposing C=C Bonds

*No Wikipedia article

EC 5.3.4: Transposing S-S Bonds

EC 5.3.99: Other Intramolecular Oxidoreductases

*No Wikipedia article

EC 5.4: Intramolecular Transferases

EC 5.4.1: Transferring Acyl Groups

*No Wikipedia article

EC 5.4.2: Phosphotransferases (Phosphomutases)

*No Wikipedia article

EC 5.4.3: Transferring Amino Groups

*No Wikipedia article

EC 5.4.4: Transferring hydroxy groups

*No Wikipedia article

EC 5.4.99: Transferring Other Groups

*No Wikipedia article

EC 5.5: Intramolecular Lyases

EC 5.5.1: Intramolecular lyases (only sub-subclass identified to date)

*No Wikipedia article

EC 5.6: Isomerases altering macromolecular conformation

EC 5.6.1: Enzymes altering polypeptide conformation or assembly

*No Wikipedia article

EC 5.6.2: Enzymes altering nucleic acid conformation

EC 5.99: Other Isomerases

EC 5.99.1: Sole sub-subclass for isomerases that do not belong in the other subclasses

Related Research Articles

In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:

This is a list of topics in molecular biology. See also index of biochemistry articles.

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<span class="mw-page-title-main">Methylmalonyl CoA epimerase</span>

Methylmalonyl CoA epimerase is an enzyme involved in fatty acid catabolism that is encoded in human by the "MCEE" gene located on chromosome 2. It is routinely and incorrectly labeled as "methylmalonyl-CoA racemase". It is not a racemase because the CoA moiety has 5 other stereocenters.

In enzymology, a cycloartenol synthase (EC 5.4.99.8) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">D-lysine 5,6-aminomutase</span>

In enzymology, D-lysine 5,6-aminomutase is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">UDP-glucose 4-epimerase</span> Class of enzymes

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

In enzymology, an UDP-glucuronate 4-epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-glucuronate 5'-epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">UDP-N-acetylglucosamine 2-epimerase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 2-epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">UDP-N-acetylglucosamine 4-epimerase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 4-epimerase is an enzyme that catalyzes the chemical reaction

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References

  1. "ExplorEnz – The Enzyme Database".
  2. McDonald, A.G.; Boyce, S.; K.F., Tipton (2009). "ExplorEnz: the primary source of the IUBMB enzyme list". Nucleic Acids Res. 37: D593–D597. doi: 10.1093/nar/gkn582 . PMC   2686581 .