| + |
Trifunctional enzyme | down-regulates quantity 
chemical modification
|
(E)-hexadec-2-enoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280310 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3- hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity 
chemical modification
|
(S)-3-hydroxypalmitoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280311 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3- hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3- hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280332 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex. The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HADHA | form complex 
binding
|
Trifunctional enzyme |
0.98 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280315 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Fatty acid β-oxidation is the major energy-producing process in all tissues and is performed by four consecutive reactions that cleave fatty acids. Mitochondrial trifunctional protein (TFP) performs the last three of these four reactions. TFP is composed of two subunits: the α-subunit contains the first two of the remaining three activities (ECH and HAD), while the β-subunit bears the KT activity (Fig. 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
(S)-3-hydroxypalmitoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280316 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
NAD(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280317 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
3-oxopalmitoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
NADH(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280319 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxopalmitoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
coenzyme A(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280322 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
myristoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280323 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
acetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280324 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
(S)-3-hydroxytetradecanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex. The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
(S)-3-hydroxytetradecanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280335 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
lauroyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280339 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxolauroyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280353 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
decanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280354 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxodecanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280373 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
octanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280374 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxooctanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280385 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
hexanoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280386 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxohexanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280406 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
butyryl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280407 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HADHB | form complex
binding
|
Trifunctional enzyme |
0.98 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Fatty acid β-oxidation is the major energy-producing process in all tissues and is performed by four consecutive reactions that cleave fatty acids. Mitochondrial trifunctional protein (TFP) performs the last three of these four reactions. TFP is composed of two subunits: the α-subunit contains the first two of the remaining three activities (ECH and HAD), while the β-subunit bears the KT activity (Fig. 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | up-regulates quantity
chemical modification
|
3-oxotetradecanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280336 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
3-oxotetradecanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280338 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
trans-tetradec-2-enoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex. The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. |
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| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
Trifunctional enzyme