Glycine is an amino acid with various important functions within your body, including detoxification, DNA formation, the synthesis of hemoglobin, and as a part of brain neurotransmission pathways. Glycine and serine are interchangeable.

Glycine is a nonessential amino acid that is synthesized from choline, serine, hydroxyproline, and threonine.

It has many important physiologic functions. It is one of three amino acids that make up glutathione. Glycine’s dietary sources include meat, fish, legumes, and gelatins.

Glycine is a major collagen and elastin component, which are the most abundant proteins in the body.

Like taurine, it is an amino acid necessary for bile acid conjugation; therefore, it plays a key role in lipid digestion and absorption.

Glycine is the precursor to various important metabolites such as porphyrins, purines, heme, and creatine. It acts both as an inhibitory neurotransmitter in the CNS and as an excitatory neurotransmitter on N-methyl-D-aspartate (NMDA) receptors.

Glycine is a nonessential amino acid that is synthesized from choline, serine, hydroxyproline, and threonine. It has many important physiologic functions. It is one of three amino acids that make up glutathione. Glycine’s dietary sources include meat, fish, legumes, and gelatins. Glycine is a major collagen and elastin component, which are the most abundant proteins in the body. Like taurine, it is an amino acid necessary for bile acid conjugation; therefore, it plays a key role in lipid digestion and absorption.

Glycine is an amino acid with various important functions within your body, including detoxification, DNA formation, the synthesis of hemoglobin, and as a part of brain neurotransmission pathways. Glycine and serine are interchangeable.

Glycine is a nonessential amino acid that is synthesized from choline, serine, hydroxyproline, and threonine.

It has many important physiologic functions. It is one of three amino acids that make up glutathione. Glycine’s dietary sources include meat, fish, legumes, and gelatins.

Glycine is a major collagen and elastin component, which are the most abundant proteins in the body.

Like taurine, it is an amino acid necessary for bile acid conjugation; therefore, it plays a key role in lipid digestion and absorption.

Glycine is the precursor to various important metabolites such as porphyrins, purines, heme, and creatine. It acts both as an inhibitory neurotransmitter in the CNS and as an excitatory neurotransmitter on N-methyl-D-aspartate (NMDA) receptors.

Glycine is a nonessential amino acid that is synthesized from choline, serine, hydroxyproline, and threonine. It has many important physiologic functions. It is one of three amino acids that make up glutathione. Glycine’s dietary sources include meat, fish, legumes, and gelatins. Glycine is a major collagen and elastin component, which are the most abundant proteins in the body. Like taurine, it is an amino acid necessary for bile acid conjugation; therefore, it plays a key role in lipid digestion and absorption.

Glycine plays an important role in the body’s ability to detoxify itself as well as in wound healing. It is also important in the creation of nucleic acids and bile acids.

Glycine is the simplest amino acid and is classified as non-essential because the body can synthesize it from other compounds. Beyond its structural roles (e.g., collagen and glutathione synthesis), glycine functions as an inhibitory neurotransmitter in the spinal cord, brainstem, and retina. Loss of glycinergic inhibition—such as with tetanus toxin, which blocks the release of inhibitory transmitters—can cause spastic paralysis due to unopposed muscle contraction. Glycine also serves as a co-agonist at NMDA receptors, where it is required alongside glutamate for receptor activation.

Glycine is an amino acid with various important functions within your body, including detoxification, DNA formation, the synthesis of hemoglobin, and as a part of brain neurotransmission pathways. Glycine and serine are interchangeable.

Glycine is an amino acid with various important functions within your body, including detoxification, DNA formation, the synthesis of hemoglobin, and as a part of brain neurotransmission pathways. Glycine and serine are interchangeable.

Glycolate is one of the oxalate markers.

Glycolic acid (glycolate) is an indicator of genetic disease of oxalate metabolism called Hyperoxaluria type I due to a deficiency in the enzyme activity of alanine glyoxylate amino transferase (AGT).

Oxalate (and its acid form, oxalic acid), is an organic acid that is primarily derived from three sources: the diet, fungus (such as Aspergillus and Penicillium), possibly Candida, and also human metabolism.

Oxalic acid is the most acidic organic acid in body fluids and is used commercially to remove rust from car radiators. Antifreeze (ethylene glycol) is toxic primarily because it is converted to oxalate in the body. Two different types of genetic diseases are known in which oxalates are high in the urine, hyperoxalurias type I and type II.

In the genetic disease hyperoxaluria type I and in vitamin B-6 deficiency, there is a deficiency in the enzyme activity of alanine glyoxylate amino transferase (AGT), leading to the accumulation of glyoxylic acid. The high glyoxylic acid can then be converted to glycolate by the enzyme GRHPR or to oxalate by the enzyme LDH. Thus, glycolate, glyoxylate, and oxalate are the metabolites that are then elevated in the Organic Acids Test in hyperoxaluria type I and in vitamin B-6 deficiency. 

Indicator of genetic disease of oxalate metabolism called Hyperoxaluria type I due to a deficiency in the enzyme activity of alanine glyoxylate amino transferase (AGT).

Glycolic acid is another byproduct of the oxalate pathway and comes from the conversion of glyoxylic acid. Urinary levels of glycolic acid have most commonly been studied in the rare inborn error of metabolism primary hyperoxaluria type 1 (PH1). PH1 is caused by a deficiency of alanine:glyoxylate aminotransferase (AGT) which converts glyoxylic acid into glycine. When this pathway is blocked, due to inborn error, glyoxylic acid ultimately leads to higher production of glycolic acid and oxalic acid.

Indicator of genetic disease of oxalate metabolism called Hyperoxaluria type I due to a deficiency in the enzyme activity of alanine glyoxylate amino transferase (AGT).

Glycolic acid is another byproduct of the oxalate pathway and comes from the conversion of glyoxylic acid. Urinary levels of glycolic acid have most commonly been studied in the rare inborn error of metabolism primary hyperoxaluria type 1 (PH1). PH1 is caused by a deficiency of alanine:glyoxylate aminotransferase (AGT) which converts glyoxylic acid into glycine.