Ectoine synthase

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Ectoine synthase
Identifiers
EC no. 4.2.1.108
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The enzyme ectoine synthase (EC ) catalyzes the chemical reaction

(2S)-4-acetamido-2-aminobutanoate L-ectoine + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (2S)-4-acetamido-2-aminobutanoate (L-ectoine-forming). Other names in common use include N-acetyldiaminobutyrate dehydratase, N-acetyldiaminobutanoate dehydratase, L-ectoine synthase, EctC, and 4-N-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming). This enzyme participates in glycine, serine and threonine metabolism.

Related Research Articles

<span class="mw-page-title-main">Ectoine</span> Chemical compound

Ectoine is a natural compound found in several species of bacteria. It is a compatible solute which serves as a protective substance by acting as an osmolyte and thus helps organisms survive extreme osmotic stress. Ectoine is found in high concentrations in halophilic microorganisms and confers resistance towards salt and temperature stress. Ectoine was first identified in the microorganism Ectothiorhodospira halochloris, but has since been found in a wide range of Gram-negative and Gram-positive bacteria. Other species of bacteria in which ectoine was found include:

In enzymology, a phenylacetaldoxime dehydratase (EC 4.99.1.7) is an enzyme that catalyzes the chemical reaction

The enzyme 2-methylcitrate dehydratase (EC 4.2.1.79) catalyzes the chemical reaction

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

The enzyme 3-dehydroquinate dehydratase (EC 4.2.1.10) catalyzes the chemical reaction

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

Arogenate dehydratase (ADT) (EC 4.2.1.91) is an enzyme that catalyzes the chemical reaction

The enzyme dihydroxy-acid dehydratase (EC 4.2.1.9) catalyzes the chemical reaction

The enzyme D(−)-tartrate dehydratase (EC 4.2.1.81) catalyzes the chemical reaction

The enzyme dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) catalyzes the chemical reaction

<span class="mw-page-title-main">GDP-mannose 4,6-dehydratase</span>

The enzyme GDP-mannose 4,6-dehydratase (EC 4.2.1.47) catalyzes the chemical reaction

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

The enzyme prephenate dehydratase (EC 4.2.1.51) catalyzes the chemical reaction

The enzyme (S)-norcoclaurine synthase (EC 4.2.1.78) catalyzes the chemical reaction

In enzymology, a diaminobutyrate acetyltransferase (EC 2.3.1.178) is an enzyme that catalyzes the chemical reaction

In enzymology, a diaminobutyrate-2-oxoglutarate transaminase is an enzyme that catalyzes the chemical reaction

Zwittermicin A is an antibiotic that has been identified from the bacterium Bacillus cereus UW85. It is a molecule of interest to agricultural industry because it has the potential to suppress plant disease due to its broad spectrum activity against certain gram positive and gram negative prokaryotic micro-organisms. The molecule is also of interest from a metabolic perspective because it represents a new structural class of antibiotic and suggests a crossover between polyketide and non-ribosomal peptide biosynthetic pathways. Zwittermicin A is linear aminopolyol.

<span class="mw-page-title-main">6-carboxytetrahydropterin synthase</span> Enzyme

6-carboxytetrahydropterin synthase (EC 4.1.2.50, CPH4 synthase, queD (gene), ToyB, ykvK (gene)) is an enzyme with systematic name 7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming). This enzyme catalyses the following reversible chemical reaction.

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting) (EC 4.2.1.115, FlaA1, UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase, PseB, UDP-N-acetylglucosamine hydro-lyase (inverting, UDP-2-acetamido-2,6-dideoxy-β-L)arabino-hex-4-ulose-forming)) is an enzyme with systematic name UDP-N-acetyl-α-D-glucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose-forming). This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) (EC 4.2.1.135, PglF) is an enzyme with systematic name UDP-N-acetyl-α-Dglucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-α-Dxylo-hex-4-ulose-forming). This enzyme catalyses the following chemical reaction

2-deoxy-scyllo-Inosose synthase is an enzyme with systematic name D-glucose-6-phosphate phosphate-lyase (2-deoxy-scyllo-inosose-forming). 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

Marinococcus halophilus is a Gram-positive and halophilic bacterium from the genus of Marinococcus which has been isolated from a salted mackerel. Marinococcus halophilus produces ectoine.

References


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