id: P23378
gene_symbol: GLDC
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  GLDC is the P protein (glycine decarboxylase) of the mitochondrial glycine
  cleavage system (GCS), a pyridoxal-5'-phosphate (PLP)-dependent homodimeric
  enzyme (EC 1.4.4.2) encoded on human chromosome 9. It catalyses the first,
  committed step of glycine catabolism: it binds the alpha-amino group of glycine
  through its PLP cofactor (covalently attached as a Schiff base to Lys754),
  decarboxylates the glycine to release CO2, and transfers the residual
  aminomethyl moiety to the lipoic-acid (lipoamide) arm of the H protein (GCSH)
  rather than releasing free methylamine. Together with the T protein (AMT), the
  L protein (DLD) and the H protein (GCSH), GLDC forms the glycine cleavage
  system, the major route of glycine degradation, which links glycine to
  one-carbon/folate metabolism and serine biosynthesis. The mature protein
  localises to the mitochondrial matrix after cleavage of an N-terminal transit
  peptide. Loss-of-function variants in GLDC are the most common cause (~80% of
  cases) of nonketotic hyperglycinemia (glycine encephalopathy), an autosomal
  recessive disorder characterised by accumulation of glycine in body fluids,
  neonatal seizures and severe encephalopathy.
existing_annotations:
- term:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Core molecular function. The phylogenetic (IBA) annotation to glycine
      dehydrogenase (decarboxylating) activity is the correct, informative MF for
      the GCS P protein and is corroborated by experimental and TAS evidence in
      this same gene.
    action: ACCEPT
    reason: >-
      GLDC is the P protein of the glycine cleavage system and catalyses the
      PLP-dependent decarboxylation of glycine (EC 1.4.4.2). This IBA is
      concordant with the EXP, IDA and TAS annotations to the same term.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "The P protein (GLDC) binds the alpha-amino group of glycine"
- term:
    id: GO:0019464
    label: glycine decarboxylation via glycine cleavage system
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Core biological process. This is the most specific process term for GLDC:
      glycine decarboxylation carried out as the P-protein step of the glycine
      cleavage system.
    action: ACCEPT
    reason: >-
      Matches the experimentally established role of GLDC as the P protein of the
      GCS and is the preferred, most-informative process term for this gene.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "remaining methylamine moiety is then transferred to the lipoamide"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: >-
      Correct subcellular localisation. GLDC acts in the mitochondrion (matrix).
      This IBA is consistent with IDA, HTP and TAS localisation evidence.
    action: ACCEPT
    reason: >-
      GLDC carries an N-terminal mitochondrial transit peptide and the GCS
      operates in the mitochondrial matrix; mitochondrion is the correct compartment,
      though the matrix (GO:0005759) is more precise.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Electronic assignment of the core catalytic MF via EC 1.4.4.2 / RHEA:24304
      and InterPro. Correct and concordant with experimental evidence.
    action: ACCEPT
    reason: >-
      The EC/RHEA and InterPro mappings correctly capture the glycine
      dehydrogenase (decarboxylating) activity of the P protein.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "EC=1.4.4.2"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: >-
      Electronic localisation from the UniProt Subcellular Location vocabulary
      (SL-0173, Mitochondrion). Correct.
    action: ACCEPT
    reason: >-
      Consistent with the curated UniProt subcellular location and with IDA/HTP/TAS
      evidence.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0006520
    label: amino acid metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      Very general parent process. GLDC does participate in amino acid metabolism,
      but this is far broader than its actual role in glycine cleavage.
    action: ACCEPT
    reason: >-
      Correct as a broad InterPro-based grouping term; the informative process is
      the more specific GO:0019464 (glycine decarboxylation via glycine cleavage
      system). Broad IEA parents may be retained.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "The glycine cleavage system catalyzes the degradation of"
- term:
    id: GO:0006544
    label: glycine metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      Broad but correct grouping term. GLDC is central to glycine metabolism;
      GO:0019464 is the more specific catabolic term.
    action: ACCEPT
    reason: >-
      Accurate InterPro-based parent term consistent with the enzyme acting on
      glycine.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "The glycine cleavage system catalyzes the degradation of"
- term:
    id: GO:0006546
    label: glycine catabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      Correct process: GLDC catalyses the first step of glycine degradation. This
      is the direct parent of the more specific GO:0019464.
    action: ACCEPT
    reason: >-
      Glycine catabolic process accurately describes the pathway GLDC initiates;
      concordant with IDA and TAS annotations to the same term.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "The glycine cleavage system catalyzes the degradation of"
- term:
    id: GO:0016829
    label: lyase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      Wrong-branch electronic mapping. GLDC is classified EC 1.4.4.2, an
      oxidoreductase acting on the CH-NH2 group of donors (glycine dehydrogenase
      (decarboxylating)); it is not a lyase. The lyase term derives from the broad
      PLP-fold InterPro signature IPR001597 (aromatic-amino-acid beta-eliminating
      lyase / threonine aldolase), which over-generalises to a lyase MF that does
      not apply to this enzyme.
    action: REMOVE
    reason: >-
      This is a demonstrably incorrect electronic (IEA/InterPro) MF inference: the
      enzyme's molecular function is glycine dehydrogenase (decarboxylating)
      activity (GO:0004375, an oxidoreductase, EC 1.4.4.2), captured accurately by
      other annotations. Lyase activity is the wrong ontology branch for this
      protein and is safe to remove per the IEA-mis-mapping criterion.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "EC=1.4.4.2"
- term:
    id: GO:0005960
    label: glycine cleavage complex
  evidence_type: NAS
  original_reference_id: PMID:28244183
  qualifier: part_of
  review:
    summary: >-
      Correct complex membership. GLDC is the P protein subunit of the
      four-protein glycine cleavage system (P/GLDC, T/AMT, L/DLD, H/GCSH).
    action: ACCEPT
    reason: >-
      Well-established: GLDC is a bona fide subunit of the glycine cleavage
      complex. Curated by ComplexPortal.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "P (GLDC), T (GCST), L (DLD) and H (GCSH)"
- term:
    id: GO:0019464
    label: glycine decarboxylation via glycine cleavage system
  evidence_type: NAS
  original_reference_id: PMID:24467211
  qualifier: involved_in
  review:
    summary: >-
      Core process, independently supported by the mechanistic study of Go et al.
      (2014), which shows GLDC decarboxylates glycine and hands the aminomethyl
      group to the H protein within the GCS.
    action: ACCEPT
    reason: >-
      The cited mechanistic paper directly characterises GLDC-catalysed glycine
      decarboxylation as the P-protein step of the glycine cleavage system.
    supported_by:
    - reference_id: PMID:24467211
      supporting_text: "aminomethyl moiety is instead transferred to an accessory H-protein"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: >-
      Immunofluorescence (HPA) localisation to mitochondrion. Consistent with all
      other localisation evidence.
    action: ACCEPT
    reason: >-
      Direct immunofluorescence evidence supports mitochondrial localisation,
      concordant with the transit peptide and matrix localisation.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  evidence_type: EXP
  original_reference_id: PMID:1993704
  qualifier: enables
  review:
    summary: >-
      Experimental support for the core catalytic function. Kume et al. cloned the
      human glycine decarboxylase cDNA and characterised the PLP-binding
      active-site region essential for enzyme activity.
    action: ACCEPT
    reason: >-
      Direct experimental characterisation of human glycine decarboxylase,
      including the PLP-binding lysine and glycine-rich phosphate-binding region
      that organise the active site.
    supported_by:
    - reference_id: PMID:1993704
      supporting_text: "The pyridoxal phosphate binding site lysine and a glycine-rich region"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: >-
      High-throughput mitochondrial proteomics localises GLDC to mitochondria,
      concordant with all other localisation evidence.
    action: ACCEPT
    reason: >-
      GLDC was identified in a high-confidence quantitative human mitochondrial
      proteome; this HTP evidence agrees with the transit peptide, IDA
      immunofluorescence and matrix TAS annotations.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5693967
  qualifier: located_in
  review:
    summary: >-
      Most precise localisation: the glycine decarboxylation reaction occurs in
      the mitochondrial matrix. Retained as the informative compartment.
    action: ACCEPT
    reason: >-
      The GCS operates in the mitochondrial matrix; Reactome places the
      GLDC-catalysed decarboxylation there. This is the preferred, more specific
      cellular-component term.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0036255
    label: response to methylamine
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: >-
      Peripheral regulatory response inferred by similarity from rat (P15505).
      Reflects that GCS P-protein activity is inhibited in the presence of
      methylamine, not a distinct biological role of GLDC.
    action: KEEP_AS_NON_CORE
    reason: >-
      Derived from an activity-regulation observation (methylamine inhibits the
      enzyme). It is a plausible ISS-transferred response but does not represent a
      core function of GLDC; retained as non-core.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "Inhibited in presence"
- term:
    id: GO:0042803
    label: protein homodimerization activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: >-
      Supported: the functional P protein is a homodimer. Retained as a supporting
      (non-core) molecular function underpinning the catalytic unit.
    action: KEEP_AS_NON_CORE
    reason: >-
      UniProt records GLDC as a homodimer (by similarity to rat P15505), and the
      PLP-dependent active site is formed in the dimer. Real but ancillary to the
      catalytic MF.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "Homodimer (By similarity)"
- term:
    id: GO:0070280
    label: pyridoxal binding
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: >-
      The cofactor is pyridoxal 5'-phosphate (PLP), covalently bound as a Schiff
      base at Lys754, not free pyridoxal. The more accurate MF is pyridoxal
      phosphate binding (GO:0030170), which UniProt itself also carries.
    action: MODIFY
    reason: >-
      GLDC binds pyridoxal 5'-phosphate (the phosphorylated, active cofactor),
      attached as N6-(pyridoxal phosphate)lysine at Lys754; the specific,
      accurate term is GO:0030170 pyridoxal phosphate binding rather than the more
      general pyridoxal binding.
    proposed_replacement_terms:
    - id: GO:0030170
      label: pyridoxal phosphate binding
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "Name=pyridoxal 5'-phosphate"
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "N6-(pyridoxal phosphate)lysine"
- term:
    id: GO:1903442
    label: response to lipoic acid
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: >-
      Peripheral regulatory response inferred by similarity from rat (P15505),
      reflecting that P-protein activity is stimulated by lipoic acid (the
      lipoamide arm of the H protein is the physiological acceptor).
    action: KEEP_AS_NON_CORE
    reason: >-
      Derived from an activity-regulation observation (lipoic acid stimulates the
      enzyme). Consistent with the mechanism but not a core function; retained as
      non-core.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "Stimulated by lipoic acid"
- term:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  evidence_type: IDA
  original_reference_id: PMID:28244183
  qualifier: enables
  review:
    summary: >-
      Direct experimental support for the core catalytic MF: enzymatic assays of
      GCS P-protein activity for wild-type and NKH missense variants expressed in
      COS7 cells.
    action: ACCEPT
    reason: >-
      Bravo-Alonso et al. measured residual GCS P-protein (glycine decarboxylase)
      activity for GLDC constructs, directly assaying this molecular function.
    supported_by:
    - reference_id: PMID:28244183
      supporting_text: "assess the residual activity and mutant protein stability"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:28244183
  qualifier: located_in
  review:
    summary: >-
      Direct evidence of mitochondrial localisation; the same study also reported
      NKH variants with altered (partially cytosolic) localisation, confirming the
      wild-type mitochondrial targeting.
    action: ACCEPT
    reason: >-
      Localisation of GLDC to mitochondria was directly assessed; consistent with
      the transit peptide and all other localisation evidence.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0006546
    label: glycine catabolic process
  evidence_type: IDA
  original_reference_id: PMID:28244183
  qualifier: involved_in
  review:
    summary: >-
      Direct evidence linking GLDC to glycine catabolism: NKH variants cause loss
      or reduction of glycine catabolic process, as characterised functionally in
      this study.
    action: ACCEPT
    reason: >-
      The functional assessment demonstrates that pathogenic GLDC variants impair
      the glycine catabolic process, confirming GLDC's role in it. The more
      specific term is GO:0019464.
    supported_by:
    - reference_id: PMID:28244183
      supporting_text: "assess the residual activity and mutant protein stability"
- term:
    id: GO:0009055
    label: electron transfer activity
  evidence_type: TAS
  original_reference_id: PMID:2268343
  qualifier: enables
  review:
    summary: >-
      Likely over-annotation / mis-assignment. GLDC is a PLP-dependent glycine
      decarboxylase (EC 1.4.4.2); it does not act as an electron carrier. Within
      the glycine cleavage system, the redox/electron-transfer role belongs to the
      L protein (DLD, dihydrolipoamide dehydrogenase, FAD-dependent), not to the P
      protein. The cited reference (Sakakibara et al. 1990) is about a genomic
      deletion of the glycine decarboxylase gene in an NKH patient and provides no
      support for an electron transfer activity.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      The molecular function of GLDC is glycine dehydrogenase (decarboxylating)
      activity, captured by multiple experimental and electronic annotations;
      electron transfer activity is not a function of the P protein and is not
      supported by the cited paper. Flagged as over-annotated rather than removed
      because it is an author-statement (TAS) annotation whose full text was not
      reviewed.
    supported_by:
    - reference_id: file:human/GLDC/GLDC-uniprot.txt
      supporting_text: "The P protein (GLDC) binds the alpha-amino group of glycine"
- term:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  evidence_type: TAS
  original_reference_id: PMID:1996985
  qualifier: enables
  review:
    summary: >-
      Author-stated support for the core catalytic function: expression of normal
      human P-protein cDNA in COS7 cells reconstituted glycine decarboxylase
      activity comparable to human liver, whereas the NKH mutant (Phe756del) had
      none.
    action: ACCEPT
    reason: >-
      Kure et al. demonstrated glycine decarboxylase activity for the wild-type
      human enzyme and its abolition by an NKH-causing deletion, supporting the
      catalytic MF.
    supported_by:
    - reference_id: PMID:1996985
      supporting_text: "showed no activity, indicating that the three-base deletion could cause NKH"
- term:
    id: GO:0006546
    label: glycine catabolic process
  evidence_type: TAS
  original_reference_id: PMID:1996985
  qualifier: involved_in
  review:
    summary: >-
      Author-stated support that GLDC drives glycine catabolism: loss of P-protein
      activity from an NKH deletion causes the glycine-accumulation phenotype,
      linking the enzyme to the glycine catabolic process.
    action: ACCEPT
    reason: >-
      Consistent with GLDC's role in glycine degradation; the loss-of-activity
      mutant establishes the connection to glycine catabolism. GO:0019464 is the
      more specific term.
    supported_by:
    - reference_id: PMID:1996985
      supporting_text: "showed no activity, indicating that the three-base deletion could cause NKH"
core_functions:
- description: >-
    Pyridoxal-5'-phosphate-dependent decarboxylation of glycine as the P protein
    of the mitochondrial glycine cleavage system: releases CO2 from glycine and
    transfers the residual aminomethyl group to the lipoamide arm of the H protein
    (GCSH).
  molecular_function:
    id: GO:0004375
    label: glycine dehydrogenase (decarboxylating) activity
  directly_involved_in:
  - id: GO:0019464
    label: glycine decarboxylation via glycine cleavage system
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: file:human/GLDC/GLDC-uniprot.txt
    supporting_text: "The P protein (GLDC) binds the alpha-amino group of glycine"
  - reference_id: PMID:24467211
    supporting_text: "aminomethyl moiety is instead transferred to an accessory H-protein"
- description: >-
    Binds the pyridoxal 5'-phosphate cofactor (covalently attached as a Schiff
    base at Lys754) required for glycine decarboxylation.
  molecular_function:
    id: GO:0030170
    label: pyridoxal phosphate binding
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: file:human/GLDC/GLDC-uniprot.txt
    supporting_text: "N6-(pyridoxal phosphate)lysine"
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000052
  title: Gene Ontology annotation based on curation of immunofluorescence data
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/GLDC/GLDC-uniprot.txt
  title: UniProtKB entry P23378 (GCSP_HUMAN), Glycine dehydrogenase (decarboxylating),
    mitochondrial
  findings: []
- id: PMID:1993704
  title: The glycine cleavage system. Molecular cloning of the chicken and human glycine
    decarboxylase cDNAs and some characteristics involved in the deduced protein structures.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Abstract-only cache; PubMed-verified. Cloned human glycine decarboxylase cDNA
      and characterised the PLP-binding active-site region. Supports the catalytic
      MF and PLP cofactor role.
- id: PMID:1996985
  title: 'Structural and expression analyses of normal and mutant mRNA encoding glycine
    decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Abstract-only cache; PubMed-verified. WT human P-protein cDNA reconstituted
      glycine decarboxylase activity in COS7; NKH Phe756del abolished it. Supports
      catalytic MF and glycine catabolic process.
- id: PMID:2268343
  title: One of the two genomic copies of the glycine decarboxylase cDNA has been
    deleted at a 5' region in a patient with nonketotic hyperglycinemia.
  findings: []
  reference_review:
    relevance: LOW
    correctness: MISCITED
    review_notes: >-
      Abstract-only cache; PubMed-verified. The paper describes a genomic deletion
      of the glycine decarboxylase gene in an NKH patient and does NOT support the
      electron transfer activity (GO:0009055) it is cited for; that MF annotation is
      an over-annotation/mis-assignment for the P protein.
- id: PMID:24467211
  title: Glycine decarboxylase is an unusual amino acid decarboxylase involved in
    tumorigenesis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Abstract-only cache; PubMed-verified. Mechanistic study showing GLDC is an
      unusual PLP-dependent alpha-amino acid decarboxylase that removes CO2 without
      releasing free methylamine and transfers the aminomethyl group to the H
      protein. Directly supports the GCS decarboxylation function.
- id: PMID:28244183
  title: 'Nonketotic hyperglycinemia: Functional assessment of missense variants in
    GLDC to understand phenotypes of the disease.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Abstract-only cache; PubMed-verified. Enzymatic assays of GCS P-protein
      activity and structural modelling for 19 GLDC missense variants; supports the
      catalytic MF, glycine catabolic process, mitochondrial localisation and
      complex membership.
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics
    in cellular context.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Abstract-only cache (GLDC data in supplementary tables not present in the
      cache). High-throughput mitochondrial proteomics; supports mitochondrial
      localisation of GLDC.
- id: Reactome:R-HSA-5693967
  title: PXLP-K754-GLDC dimer decarboxylates Gly
  findings: []