PHYKPL

PHYKPL

Target · Mitochondrial enzyme

PHYKPL 5-phosphohydroxy-L-lysine phospho-lyase · alanine-glyoxylate aminotransferase 2-like 2

PHYKPL (5-phosphohydroxy-L-lysine phospho-lyase) is a pyridoxal-phosphate-dependent mitochondrial enzyme that breaks down 5-phosphohydroxy-L-lysine. It was previously named AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) and is also known as MGC15875. Browse Assay Genie's current range of PHYKPL research reagents below, or read on for the biology behind the target.

Mitochondrial enzymePyridoxal-phosphate lyaseLinked to phosphohydroxylysinuria
450 aa
Protein length
~50 kDa
Molecular weight
5q35.3
Gene locus
EC 4.2.3.134
Enzyme class
Target information

What is PHYKPL (5-phosphohydroxy-L-lysine phospho-lyase)?

PHYKPL catalyses the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine. The reaction converts this substrate into ammonia, inorganic phosphate and 2-aminoadipate semialdehyde. The enzyme is assigned EC 4.2.3.134 and sits within the HGNC gene group of carbon-oxygen lyases, reflecting its lyase activity on a phosphate ester.

The PHYKPL gene is a nuclear gene that encodes a mitochondrial enzyme, and UniProt records its subcellular location as the mitochondrion. The protein belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. According to the NCBI Gene summary, alternative splicing of the gene produces multiple transcript variants. A mouse ortholog, Phykpl, is recorded in the data for this target.

The gene was formerly designated AGXT2L2, after alanine-glyoxylate aminotransferase 2-like 2, a name that reflects its sequence relationship to aminotransferases rather than its present assigned activity. It is also listed under the alias MGC15875. Per the NCBI Gene summary, mutations in this gene may cause phosphohydroxylysinuria, which makes PHYKPL of interest to researchers studying lysine-derived metabolites and the inherited disorders that affect their handling.

Lysine catabolism research

PHYKPL converts 5-phosphohydroxy-L-lysine to 2-aminoadipate semialdehyde, ammonia and inorganic phosphate, so it is a point of study in lysine-related metabolism.

Phosphohydroxylysinuria studies

Mutations in the PHYKPL gene may cause phosphohydroxylysinuria, making the enzyme relevant to work on this inherited metabolic condition.

Mitochondrial enzymology

As a nuclear-encoded enzyme that acts in the mitochondrion, PHYKPL is a useful subject for studying mitochondrial metabolic enzymes.

Pyridoxal-phosphate enzyme biology

PHYKPL belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family and uses this cofactor to catalyse a lyase reaction.

Background

PHYKPL frequently asked questions

What does PHYKPL do?

PHYKPL is a mitochondrial enzyme that catalyses the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine. The products are ammonia, inorganic phosphate and 2-aminoadipate semialdehyde. It is classified as EC 4.2.3.134, a carbon-oxygen lyase.

What other names does PHYKPL go by?

The HGNC-approved name is 5-phosphohydroxy-L-lysine phospho-lyase. The gene was previously called AGXT2L2, for alanine-glyoxylate aminotransferase 2-like 2, and the alias MGC15875 is also listed. The NCBI Gene summary notes that alternative splicing yields multiple transcript variants.

Is PHYKPL linked to disease or conserved in other species?

The NCBI Gene summary states that mutations in PHYKPL may cause phosphohydroxylysinuria. A mouse ortholog, Phykpl, is recorded for this gene. Check the datasheet of any product for its validated reactivity.

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Related targets

Other pyridoxal-phosphate-dependent enzymes and lysine-metabolism proteins with products at Assay Genie.

Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8IUZ5; product specifications from Assay Genie datasheets.

PHYKPL Product listing

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