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Your query returned 8 entries. Printable version
EC | 6.2.1.7 | ||||||||||||||
Accepted name: | cholate—CoA ligase | ||||||||||||||
Reaction: | (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA (2) ATP + (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA |
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For diagram of cholic acid conjugates biosynthesis, click here and for diagram of cholic acid biosynthesis (sidechain), click here | |||||||||||||||
Glossary: | cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate trihydroxycoprostanoate = 3α,7α,12α-trihydroxy-5β-cholestan-26-oate |
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Other name(s): | BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate—CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase | ||||||||||||||
Systematic name: | cholate:CoA ligase (AMP-forming) | ||||||||||||||
Comments: | Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates [7]. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway [5]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-90-1 | ||||||||||||||
References: |
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EC | 6.2.1.70 | ||||||||||||||
Accepted name: | L-threonine—[L-threonyl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + L-threonine + holo-[L-threonyl-carrier protein] = AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein] (overall reaction) (1a) ATP + L-threonine = diphosphate + (L-threonyl)adenylate (1b) (L-threonyl)adenylate + holo-[L-threonyl-carrier protein] = AMP + L-threonyl-[L-threonyl-carrier protein] |
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Other name(s): | dhbF (gene name); pmsD (gene name); syrB1 (gene name) | ||||||||||||||
Systematic name: | L-threonine:[L-threonyl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of L-threonine to (L-threonyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein (as in the case of DhbF in bacillibactin biosynthesis), or of a different protein (as in the case of PmsD in pseudomonine biosynthesis). This activity is often found as part of a larger non-ribosomal peptide synthase. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
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EC | 6.2.1.71 | ||||||||||||||
Accepted name: | 2,3-dihydroxybenzoate—[aryl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + 2,3-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 2,3-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction) (1a) ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate (1b) (2,3-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 2,3-dihydroxybenzoyl-[aryl-carrier protein] |
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Other name(s): | entE (gene name); vibE (gene name); dhbE (gene name); angE (gene name) | ||||||||||||||
Systematic name: | 2,3-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of 2,3-dihydroxybenzoate to (2,3-dihydroxybenzoyl)adenylate, followed by the transfer the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain of a specific non-ribosomal peptide synthase. For example, the EntE enzyme of Escherichia coli is part of the enterobactin synthase complex, the VibE enzyme of Vibrio cholerae is part of the vibriobactin synthase complex, and the DhbE enzyme of Bacillus subtilis is part of the bacillibactin synthase complex. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
References: |
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EC | 6.2.1.72 | ||||||||||||||
Accepted name: | L-serine—[L-seryl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + L-serine + holo-[L-seryl-carrier protein] = AMP + diphosphate + L-seryl-[L-seryl-carrier protein] (overall reaction) (1a) ATP + L-serine = diphosphate + (L-seryl)adenylate (1b) (L-seryl)adenylate + holo-[L-seryl-carrier protein] = AMP + L-seryl-[L-seryl-carrier protein] |
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Other name(s): | entF (gene name); zmaJ (gene name); gdnB (gene name); serine-activating enzyme | ||||||||||||||
Systematic name: | L-serine:[L-seryl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of L-serine to (L-seryl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
References: |
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EC | 6.2.1.73 | ||||||||||||||
Accepted name: | L-tryptophan—[L-tryptophyl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + L-tryptophan + holo-[L-tryptophyl-carrier protein] = AMP + diphosphate + -L-tryptophyl-[L-tryptophyl-carrier protein] (overall reaction) (1a) ATP + tryptophan = diphosphate + (L-tryptophyl)adenylate (1b) (L-tryptophyl)adenylate + holo-[L-tryptophyl-carrier protein] = AMP + L-tryptophyl-[L-tryptophyl-carrier protein] |
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Other name(s): | ecm13 (gene name); swb11 (gene name) | ||||||||||||||
Systematic name: | L-tryptophan:[L-tryptophyl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of L-tryptophan to (L-tryptophyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
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EC | 6.2.1.74 | ||||||||||||||
Accepted name: | 3-amino-5-hydroxybenzoate—[acyl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] = 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate | ||||||||||||||
Other name(s): | rifA (gene name); mitE (gene name) | ||||||||||||||
Systematic name: | 3-amino-5-hydroxybenzoate:[acyl carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | During the biosynthesis of most ansamycin antibiotics such as rifamycins, streptovaricins, naphthomycins, and chaxamycins, the activity is catalysed by the loading domain of the respective polyketide synthase (PKS), which transfers the substrate to the acyl-carrier protein domain of the first extension module of the PKS. During the biosynthesis of the mitomycins the reaction is catalysed by the MitE protein, which transfers the substrate to a dedicated acyl-carrier protein (MmcB). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 6.2.1.75 | ||||||||||||||
Accepted name: | indoleacetate—CoA ligase | ||||||||||||||
Reaction: | ATP + (indol-3-yl)acetate + CoA = AMP + diphosphate + (indol-3-yl)acetyl-CoA | ||||||||||||||
Other name(s): | iaaB (gene name) | ||||||||||||||
Systematic name: | (indol-3-yl)acetate:CoA ligase (AMP-forming) | ||||||||||||||
Comments: | The enzyme, characterized from the bacterium Aromatoleum aromaticum, is involved in degradation of (indol-3-yl)acetate. It is also active with phenylacetate and the non-physiological compound (2-naphthyl)acetate. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
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EC | 6.2.1.76 | ||||||||||||||
Accepted name: | malonate—CoA ligase | ||||||||||||||
Reaction: | ATP + malonate + CoA = AMP + diphosphate + malonyl-CoA | ||||||||||||||
Other name(s): | ACSF3 (gene name); AAE13 (gene name); malonyl-CoA synthetase | ||||||||||||||
Systematic name: | malonate:CoA ligase (AMP-forming) | ||||||||||||||
Comments: | The enzyme, found in mitochondria, detoxifies malonate, which is a potent inhibitor of mitochondrial respiration, and provides malonyl-CoA to the mitochondrial fatty acid biosynthesis pathway. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
References: |
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