List of EC numbers (EC 4)

Last updated

This list contains a list of EC numbers for the fourth group, EC 4, lyases, 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 4.1: Carbon-Carbon Lyases

EC 4.1.1: Carboxy-lyases

*No Wikipedia article

EC 4.1.2: Aldehyde-lyases

*No Wikipedia article

EC 4.1.3: Oxo-Acid-Lyases

*No Wikipedia article

EC 4.1.99: Other Carbon-Carbon Lyases

*No Wikipedia article

EC 4.2: Carbon-Oxygen Lyases

EC 4.2.1: Hydro-lyases

*No Wikipedia article

EC 4.2.2: Acting on Polysaccharides

*No Wikipedia article

EC 4.2.3: Acting on phosphates

Enzymes from EC 4.2.3.141 on have no Wikipedia articles

EC 4.2.99: Other Carbon-Oxygen Lyases

*No Wikipedia article

EC 4.3: Carbon-Nitrogen Lyases

EC 4.3.1: Ammonia-Lyases

*No Wikipedia article

EC 4.3.2: Amidine-Lyases

*No Wikipedia article

EC 4.3.3: Amine-Lyases

EC 4.3.99: Other Carbon-Nitrogen Lyases

*No Wikipedia article

EC 4.4: Carbon-Sulfur Lyases

EC 4.4.1: Carbon-sulfur lyases (only sub-subclass identified to date)

*No Wikipedia article

EC 4.5: Carbon-Halide Lyases

EC 4.5.1: Carbon-halide lyases (only sub-subclass identified to date)

EC 4.6: Phosphorus-Oxygen Lyases

EC 4.6.1: Phosphorus-oxygen lyases (only sub-subclass identified to date)

*No Wikipedia article

EC 4.7: Carbon-phosphorus lyases

EC 4.7.1: Carbon-phosphorus lyases (only sub-subclass identified to date)

*No Wikipedia article

EC 4.8: Nitrogen-oxygen lyases

EC 4.8.1: Hydro-lyases

*No Wikipedia article

EC 4.98: ATP-independent chelatases

EC 4.98.1: Forming coordination complexes

EC 4.99: Other Lyases

EC 4.99.1: Sole sub-subclass for lyases that do not belong in the other subclasses

*No Wikipedia article

Related Research Articles

In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.

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

The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia:

<span class="mw-page-title-main">Cystathionine beta-lyase</span> Enzyme

Cystathionine beta-lyase, also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction

The enzyme erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) catalyzes the chemical reaction

The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction

The enzyme 2-dehydro-3-deoxy-6-phosphogalactonate aldolase catalyzes the chemical reaction

The enzyme 2-dehydro-3-deoxy-L-pentonate aldolase catalyzes the chemical reaction

<span class="mw-page-title-main">2-Dehydro-3-deoxy-phosphogluconate aldolase</span> Class of enzymes

The enzyme 2-dehydro-3-deoxy-phosphogluconate aldolase, commonly known as KDPG aldolase, catalyzes the chemical reaction

The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction

The enzyme 5-dehydro-2-deoxyphosphogluconate aldolase catalyzes the chemical reaction

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

The enzyme phosphogluconate dehydratase (EC 4.2.1.12) catalyzes the chemical reaction

In enzymology, a 3-deoxy-8-phosphooctulonate synthase (EC 2.5.1.55) is an enzyme that catalyzes the chemical reaction

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

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

<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. "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 .