Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Branched-chain-amino-acid transaminase activity. It is involved in the biological process described with: valine biosynthetic process; branched-chain amino acid biosynthetic process; leucine biosynthetic process; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial; Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

RE62833p; isovaleryl-CoA dehydrogenase activity; flavin adenine dinucleotide binding. It is involved in the biological process described with: oxidation-reduction process; leucine catabolic process.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Fumarylacetoacetase activity. It is involved in the biological process described with: L-phenylalanine catabolic process; homogentisate catabolic process; tyrosine catabolic process.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial; Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism (By similarity). Vital for adult survival.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Serine hydroxymethyl transferase (Shmt) encodes a conserved pyridoxal phosphate-containing enzyme that converts serine into glycine and N5,N10-methylentetrahydrofolate. This reaction represents a major source for activated C1 units and tetrahydrofolate-mediated C1 metabolism; Belongs to the SHMT family.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Serine racemase, isoform B; Serine racemase activity; L-serine ammonia-lyase activity; L-threonine ammonia-lyase activity. It is involved in the biological process described with: threonine catabolic process; L-serine catabolic process.

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Arginase (arg) encodes an enzyme that converts arginine into ornithine. Lack of arg produces a developmental embryonic delay.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Adenosylhomocysteinase (Ahcy) encodes S-adenosyl-L-homocysteine hydrolase, the rate-limiting enzyme in methionine metabolism. This tetrameric enzyme catalyzes the reversible hydrolysis of S-Adenosylhomocysteine (SAH) to adenosine and L-homocysteine. The function of Ahcy product is required to maintain proper concentrations of SAH, which serves as an inhibitor of S-adenosylmethionine-dependent methylation reactions.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Serine hydroxymethyl transferase (Shmt) encodes a conserved pyridoxal phosphate-containing enzyme that converts serine into glycine and N5,N10-methylentetrahydrofolate. This reaction represents a major source for activated C1 units and tetrahydrofolate-mediated C1 metabolism; Belongs to the SHMT family.

Adenosylhomocysteinase like 1 (AhcyL1) encodes a protein that, together with the product of AhcyL2, belongs to AHCY-like proteins. AhcyL1 and AhcyL2 products have lost their canonical enzymatic functions due to critical mutations in their AHCY-domains. However, via hetero-multimerization, the products of AhcyL1 and AhcyL2 can suppress the activity of the enzyme encoded by Ahcy, which catalyzes the hydrolysis of S-Adenosylhomocysteine. The presence of a N-terminal IRBIT domain confers AhcyL1 and AhcyL2 proteins new functions in Ca[2+] signaling, intracellular pH regulation and productio [...]

Serine racemase, isoform B; Serine racemase activity; L-serine ammonia-lyase activity; L-threonine ammonia-lyase activity. It is involved in the biological process described with: threonine catabolic process; L-serine catabolic process.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

FI03238p; Pyridoxal phosphate binding; glycine C-acetyltransferase activity. It is involved in the biological process described with: biosynthetic process; threonine catabolic process; cellular amino acid metabolic process.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

GH12548p; FAD binding; D-amino-acid oxidase activity. It is involved in the biological process described with: D-amino acid metabolic process; oxidation-reduction process.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

IP18034p; Pyridoxal phosphate binding; alanine-glyoxylate transaminase activity; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

Branched-chain-amino-acid transaminase activity. It is involved in the biological process described with: valine biosynthetic process; branched-chain amino acid biosynthetic process; leucine biosynthetic process; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

Glycine cleavage system P protein; The glycine cleavage system catalyzes the degradation of glycine.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

GH18546p; L-threonine 3-dehydrogenase activity; coenzyme binding. It is involved in the biological process described with: threonine catabolic process.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine; Belongs to the GcvT family.

LD34157p; L-allo-threonine aldolase activity. It is involved in the biological process described with: threonine catabolic process; glycine biosynthetic process.

Flavin adenine dinucleotide binding; dihydrolipoyl dehydrogenase activity; electron transfer activity. It is involved in the biological process described with: tricarboxylic acid cycle; lipoamide metabolic process; oxidation-reduction process; glycine catabolic process; cell redox homeostasis.