id: P15802
gene_symbol: aatA
taxon:
  id: NCBITaxon:5076
  label: Penicillium chrysogenum
description: Isopenicillin-N N-acyltransferase (IAT) that catalyzes the final step
  in penicillin biosynthesis. The enzyme exchanges the α-aminoadipyl side chain of
  isopenicillin N for phenylacetic acid to produce penicillin G. Functions as a self-processing
  enzyme that is initially synthesized as a 40 kDa precursor and undergoes autocatalytic
  cleavage to form an active heterodimer containing 11 kDa and 29 kDa subunits. Located
  in the peroxisomal matrix where penicillin biosynthesis occurs.
alternative_records:
- id: A0ABQ8WFJ5
  relationship: REFERENCE_PROTEOME_EQUIVALENT
  reference_proteome: UP001220256
  reviewed_on: '2026-10-19'
  reason: Retain P15802 as the primary Swiss-Prot accession. The 357-residue reference sequence differs
    at two residues with full ungapped coverage (99.44% identity). The other retrieved hit is distant
    and structurally dissimilar. This supports a qualified sequence-based counterpart; the source strain
    is AS-P-78 and no functional neutrality of the two substitutions is assumed.
  evidence:
  - type: PROTEOME_SEARCH
    description: MMseqs2 searched 12,232 sequences across UP001220256 at E <= 1e-5 and sensitivity 7.5,
      returning 2 hits. Every returned sequence was globally aligned using BLOSUM62 with gap-open -10
      and extension -0.5. Scores and sequences for all 2 returned candidates are retained, with 2 detailed
      alignment files. The heuristic search does not establish genomic absence or unique locus identity.
    supported_by:
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: 'target_sequence_count: 12232'
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: 'candidate_count: 2'
  - type: SEQUENCE_COMPARISON
    description: 'A0ABQ8WFJ5: 355 identities across 357 global-alignment columns (99.4398% identity including
      gaps), 2 substitutions and 0 gap columns. Query coverage is 100.0%; target coverage is 100.0%. Sequence
      similarity is interpreted in the manual rationale. Identity over paired residues is 99.4398% (355/357);
      gap columns are excluded from this denominator.'
    supported_by:
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: |-
        query_length: 357
          target_length: 357
          alignment_columns: 357
          identities: 355
          mismatches: 2
          gap_columns: 0
          identity_percent: 99.4398
          query_coverage_percent: 100.0
          target_coverage_percent: 100.0
  - type: PROTEOME_MEMBERSHIP
    description: The primary accession is outside every searched exact-taxon reference proteome. Current
      UniProt records place A0ABQ8WFJ5 in UP001220256 and give it the same taxon as the primary.
    supported_by:
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: 'primary_in_any_reference_proteome: false'
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: 'alternative_in_reference_proteome: true'
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: 'same_taxon: true'
  - type: RECORD_HISTORY
    description: 'Sampled UniSave observations: 11-NOV-2015, entry version 79.: no Proteomes cross-reference;
      12-AUG-2020, entry version 87.: no Proteomes cross-reference; 27-NOV-2024, entry version 97.: no
      Proteomes cross-reference. These dated observations do not establish uninterrupted membership/absence,
      the exact change date, or UniProt''s motivation.'
    supported_by:
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: |-
        entry_date: 11-NOV-2015, entry version 79.
          proteomes: []
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: |-
        entry_date: 12-AUG-2020, entry version 87.
          proteomes: []
    - reference_id: file:PENCH/aatA/aatA-record-evidence.yaml
      supporting_text: |-
        entry_date: 27-NOV-2024, entry version 97.
          proteomes: []
existing_annotations:
- term:
    id: GO:0005777
    label: peroxisome
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  retired: true
  review:
    summary: Correct subcellular location annotation. UniProt confirms peroxisomal
      localization with IDA evidence.
    action: ACCEPT
    supported_by:
    - reference_id: UniProt:P15802
      supporting_text: 'SUBCELLULAR LOCATION: Peroxisome matrix'
      reference_section_type: DATABASE_ENTRY
    - reference_id: file:PENCH/aatA/aatA-deep-research.md
      supporting_text: whose proper localization to microbodies is required for efficient
        antibiotic biosynthesis
- term:
    id: GO:0005782
    label: peroxisomal matrix
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  retired: true
  review:
    summary: Correct specific subcellular location annotation. UniProt confirms peroxisomal
      matrix localization with IDA evidence.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:18439860
      supporting_text: The unprocessed preprotein form IATC103S of the isopenicillin
        N acyltransferase is transported inside peroxisomes
      reference_section_type: ABSTRACT
- term:
    id: GO:0016740
    label: transferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  retired: true
  review:
    summary: Too general but correct. The enzyme has specific acyltransferase activity.
    action: KEEP_AS_NON_CORE
    supported_by:
    - reference_id: UniProt:P15802
      supporting_text: Isopenicillin-N N-acyltransferase; part of the gene cluster
        that mediates the biosynthesis of penicillin
      reference_section_type: DATABASE_ENTRY
- term:
    id: GO:0016746
    label: acyltransferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  retired: true
  review:
    summary: Correct but not specific enough. The enzyme has specific isopenicillin-N
      N-acyltransferase activity.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0050640
      label: isopenicillin-N N-acyltransferase activity
    supported_by:
    - reference_id: PMID:2120195
      supporting_text: removal of the L-alpha-aminoadipyl side chain from isopenicillin
        N (IPN) and exchange with a nonpolar side chain
      reference_section_type: ABSTRACT
- term:
    id: GO:0017000
    label: antibiotic biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  retired: true
  review:
    summary: Correct but not specific enough. The enzyme is involved in penicillin
      biosynthesis specifically.
    action: MODIFY
    proposed_replacement_terms:
    - id: GO:0042318
      label: penicillin biosynthetic process
    supported_by:
    - reference_id: PMID:1368505
      supporting_text: A cosmid clone containing the putative penicillin biosynthetic
        gene cluster from Penicillium chrysogenum
      reference_section_type: ABSTRACT
- term:
    id: GO:0042318
    label: penicillin biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Correct annotation representing the core function of this enzyme.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:2120195
      supporting_text: The final step in the biosynthesis of beta-lactam antibiotics
        in Penicillium chrysogenum and Aspergillus nidulans involves removal of the
        L-alpha-aminoadipyl side chain from isopenicillin N
      reference_section_type: ABSTRACT
  qualifier: involved_in
  supporting_entities:
  - ARBA:ARBA00087383
- term:
    id: GO:0050640
    label: isopenicillin-N N-acyltransferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: Correct and specific molecular function annotation representing the core
      enzymatic activity.
    action: ACCEPT
    supported_by:
    - reference_id: UniProt:P15802
      supporting_text: AatA catalyzes the exchange of the alpha-aminoadipyl side chain
        of isopenicillin N for phenylacetic acid to yield penicillin
      reference_section_type: DATABASE_ENTRY
  qualifier: enables
  supporting_entities:
  - ARBA:ARBA00098303
  - RHEA:20720
  - EC:2.3.1.164
- term:
    id: GO:0042318
    label: penicillin biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:2120195
  review:
    summary: Correct annotation with strong experimental evidence (IDA).
    action: ACCEPT
    supported_by:
    - reference_id: PMID:2120195
      supporting_text: Acyltransferase activity from Escherichia coli producing the
        40-kDa protein
      reference_section_type: ABSTRACT
  qualifier: involved_in
- term:
    id: GO:0005782
    label: peroxisomal matrix
  evidence_type: IDA
  original_reference_id: PMID:18439860
  review:
    summary: Correct subcellular location with strong experimental evidence (IDA).
    action: ACCEPT
    supported_by:
    - reference_id: PMID:18439860
      supporting_text: Unprocessed preprotein form IATC103S of the isopenicillin N
        acyltransferase is transported inside peroxisomes
      reference_section_type: ABSTRACT
  qualifier: is_active_in
- term:
    id: GO:0042318
    label: penicillin biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:1368505
  review:
    summary: Correct annotation with strong experimental evidence showing functional
      penicillin biosynthesis.
    action: ACCEPT
    supported_by:
    - reference_id: PMID:1368505
      supporting_text: Both of the transformed hosts contained intact P. chrysogenum
        DNA derived from the cosmid clone and produced authentic penicillin V
      reference_section_type: ABSTRACT
  qualifier: acts_upstream_of_or_within
- term:
    id: GO:0050640
    label: isopenicillin-N N-acyltransferase activity
  evidence_type: IDA
  original_reference_id: PMID:2120195
  review:
    summary: Correct and specific molecular function with strong experimental evidence
      (IDA).
    action: ACCEPT
    supported_by:
    - reference_id: PMID:2120195
      supporting_text: The enzyme catalyzing this reaction, acyl-coenzyme A:isopenicillin
        N acyltransferase (acyltransferase), was purified from P. chrysogenum
      reference_section_type: ABSTRACT
  qualifier: enables
- term:
    id: GO:0008234
    label: cysteine-type peptidase activity
  evidence_type: IEA
  review:
    summary: AatA functions as a self-processing enzyme that undergoes autocatalytic
      cleavage using Cys103 as the nucleophile to generate the active heterodimeric
      form.
    action: NEW
    reason: This molecular function term captures AatA's cysteine-dependent autoproteolytic
      activity that is essential for enzyme maturation and activation.
    supported_by:
    - reference_id: PMID:20223213
      supporting_text: Structure of a Cys103Ala precursor mutant shows that maturation
        is autoproteolytic, initiated by Cys103 cleaving its preceding peptide bond
    - reference_id: PMID:2120195
      supporting_text: The active form of the enzyme may result from processing of
        the 40-kDa monomeric precursor to a heterodimer containing subunits of 11
        and 29 kDa
    - reference_id: file:PENCH/aatA/aatA-bioinformatics/RESULTS.md
      supporting_text: All structures show cleavage between Gly102 and Cys103, creating
        heterodimeric subunits
- term:
    id: GO:0097264
    label: self proteolysis
  evidence_type: IEA
  review:
    summary: AatA undergoes autocatalytic cleavage to convert from an inactive 40
      kDa precursor to an active heterodimeric enzyme with 11 kDa and 29 kDa subunits.
    action: NEW
    reason: This biological process term describes AatA's essential autoproteolytic
      maturation step that is required for enzymatic activity in penicillin biosynthesis.
    supported_by:
    - reference_id: PMID:18439860
      supporting_text: IAT is post-translationally regulated by its preprotein, which
        interferes with the self-processing.
    - reference_id: PMID:20223213
      supporting_text: The structure of a Cys103Ala precursor mutant shows that maturation
        is autoproteolytic, initiated by Cys103 cleaving its preceding peptide bond.
    - reference_id: PMID:2120195
      supporting_text: The active form of the enzyme may result from processing of
        the 40-kDa monomeric precursor to a heterodimer containing subunits of 11
        and 29 kDa.
- term:
    id: GO:0005782
    label: peroxisomal matrix
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  supporting_entities:
  - ARBA:ARBA00088448
  - UniProtKB-SubCell:SL-0202
  review:
    summary: Combined automated (ARBA + UniProt subcellular location) peroxisomal
      matrix annotation; current replacement of the retired GO_REF:0000044 row.
      Consistent with direct localization of IAT (including the unprocessed C103S
      proenzyme) inside peroxisomes.
    action: ACCEPT
    reason: Matches the experimentally determined peroxisomal matrix localization
      (IDA, PMID:18439860), where the final step of penicillin biosynthesis occurs.
    supported_by:
    - reference_id: PMID:18439860
      supporting_text: Expression of a mutant penDE(C103S) gene in P. chrysogenum
        gave rise to an unprocessed inactive variant of IAT (IAT(C103S)) located
        inside peroxisomes
- term:
    id: GO:0050640
    label: isopenicillin-N N-acyltransferase activity
  evidence_type: EXP
  original_reference_id: PMID:1368505
  qualifier: enables
  review:
    summary: Heterologous expression of the P. chrysogenum penicillin cluster cosmid
      in N. crassa and A. niger conferred acyl-CoA:6-APA acyltransferase (ACT/IAT)
      activity together with penicillin V production. Experimental support for the
      core acyltransferase activity encoded by penDE/aatA.
    action: ACCEPT
    reason: Curator EXP annotation consistent with the purified-enzyme and recombinant
      evidence (PMID:2120195, PMID:2110531); the cosmid-based assay is indirect for
      the individual gene but the activity is unambiguously that of aatA. Abstract-only
      cache; defer to curator.
    supported_by:
    - reference_id: PMID:1368505
      supporting_text: Assays of penicillin biosynthetic enzyme activity additionally
        demonstrated that they possessed delta-(L-alpha-amino-adipyl)-L-cysteinyl-D-valine
        synthetase (ACVS), isopenicillin N synthetase (IPNS) and acyl coenzyme A:6-aminopenicillanic
        acid acyltransferase (ACT) activity
- term:
    id: GO:0050640
    label: isopenicillin-N N-acyltransferase activity
  evidence_type: EXP
  original_reference_id: PMID:2110531
  qualifier: enables
  review:
    summary: Purified P. chrysogenum/A. nidulans acyltransferase (40 kDa) transfers
      the phenylacetyl group from phenylacetyl-CoA to 6-APA and converts isopenicillin
      N to benzylpenicillin; direct enzymatic evidence for isopenicillin-N N-acyltransferase
      activity.
    action: ACCEPT
    reason: Direct assay of purified enzyme demonstrating the core catalytic activity.
    supported_by:
    - reference_id: PMID:2110531
      supporting_text: It also catalyses the conversion of isopenicillin N (IPN) to
        benzylpenicillin (Pen G) and hydrolyses IPN to 6-APA
references:
- id: file:PENCH/aatA/aatA-record-evidence.yaml
  title: Compact archived record and sequence evidence for P15802
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  full_text_unavailable: false
  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.
  full_text_unavailable: false
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  full_text_unavailable: false
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods.
  full_text_unavailable: false
  findings: []
- id: PMID:1368505
  title: Cloning and heterologous expression of the penicillin biosynthetic gene cluster
    from penicillum chrysogenum.
  findings:
  - statement: Demonstrated heterologous expression of complete penicillin biosynthetic
      gene cluster from P. chrysogenum in N. crassa and A. niger
    supporting_text: Both of the transformed hosts contained intact P. chrysogenum
      DNA derived from the cosmid clone and produced authentic penicillin V
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Confirmed production of authentic penicillin V in transformed hosts
    supporting_text: Both of the transformed hosts contained intact P. chrysogenum
      DNA derived from the cosmid clone and produced authentic penicillin V
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Showed functional expression of acyl coenzyme A:6-aminopenicillanic
      acid acyltransferase (ACT) activity
    supporting_text: possessed delta-(L-alpha-amino-adipyl)-L-cysteinyl-D-valine synthetase
      (ACVS), isopenicillin N synthetase (IPNS) and acyl coenzyme A:6-aminopenicillanic
      acid acyltransferase (ACT) activity
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Established that all genes necessary for penicillin biosynthesis from
      amino acid precursors are closely linked in P. chrysogenum
    supporting_text: The data suggests that genes encoding all the enzymes necessary
      for the biosynthesis of penicillin from amino acid precursors are closely linked
      in P. chrysogenum and constitute a gene cluster
    reference_section_type: ABSTRACT
    full_text_unavailable: true
- id: PMID:18439860
  title: The unprocessed preprotein form IATC103S of the isopenicillin N acyltransferase
    is transported inside peroxisomes and regulates its self-processing.
  findings:
  - statement: Demonstrated that unprocessed IAT(C103S) mutant is transported into
      peroxisomes, proving processing-independent transport
    supporting_text: Expression of a mutant penDE(C103S) gene in P. chrysogenum gave
      rise to an unprocessed inactive variant of IAT (IAT(C103S)) located inside peroxisomes
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Showed that IAT transport into peroxisomes does not require prior self-processing
    supporting_text: transport of the proIAT inside these organelles is not dependent
      on the processing state of the protein
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Discovered regulatory role of unprocessed IAT(C103S) in wild-type IAT
      processing
    supporting_text: Changes in the wild-type IAT processing profile (beta subunit
      formation) were observed in the Wis54-DE(C103S) strain, suggesting a regulatory
      role of the unprocessed IAT(C103S) in the processing of the wild-type IAT
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Confirmed post-translational regulation where preprotein interferes
      with self-processing
    supporting_text: Our results indicate that IAT is post-translationally regulated
      by its preprotein, which interferes with the self-processing
    reference_section_type: ABSTRACT
    full_text_unavailable: true
- id: PMID:2120195
  title: Molecular characterization of the acyl-coenzyme A:isopenicillin N acyltransferase
    gene (penDE) from Penicillium chrysogenum and Aspergillus nidulans and activity
    of recombinant enzyme in Escherichia coli.
  findings:
  - statement: Cloned and characterized penDE gene encoding acyl-coenzyme A:isopenicillin
      N acyltransferase
    supporting_text: Based on NH2-terminal amino acid sequence information, the acyltransferase
      gene (penDE) from P. chrysogenum and A. nidulans were cloned
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Located penDE immediately downstream from isopenicillin N synthetase
      gene (pcbC)
    supporting_text: In both organisms, penDE was located immediately downstream from
      the isopenicillin N synthetase gene (pcbC)
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Identified gene structure with four exons encoding 357 amino acids
      (40 kDa protein)
    supporting_text: consisted of four exons encoding an enzyme of 357 amino acids
      (approximately 40 kilodaltons [kDa])
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Demonstrated functional expression in E. coli accepting both 6-aminopenicillanic
      acid and IPN as substrates
    supporting_text: Acyltransferase activity from Escherichia coli producing the
      40-kDa protein accepted either 6-aminopenicillanic acid or IPN as the substrate
      and made a penicillinase-sensitive antibiotic in the presence of phenylacetyl
      coenzyme A
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Showed enzyme undergoes processing from 40 kDa precursor to active
      heterodimer with 11 and 29 kDa subunits
    supporting_text: The active form of the enzyme may result from processing of the
      40-kDa monomeric precursor to a heterodimer containing subunits of 11 and 29
      kDa
    reference_section_type: ABSTRACT
    full_text_unavailable: true
- id: PMID:20223213
  title: Structures of an isopenicillin N converting Ntn-hydrolase reveal different
    catalytic roles for the active site residues of precursor and mature enzyme.
  findings:
  - statement: Solved crystal structure of Cys103Ala precursor mutant confirming autoproteolytic
      maturation
    supporting_text: The structure of a Cys103Ala precursor mutant shows that maturation
      is autoproteolytic
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Demonstrated that Cys103 initiates self-processing by cleaving its
      preceding peptide bond
    supporting_text: initiated by Cys103 cleaving its preceding peptide bond
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Revealed conformational change where residues 92-102 fold outward after
      autoproteolysis
    supporting_text: The crystal structure of the mature enzyme shows that after autoproteolysis
      residues 92-102 fold outwards, exposing a buried pocket
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Identified structurally flexible pocket that accommodates substrates
      of different size and polarity
    supporting_text: This pocket is structurally and chemically flexible and can accommodate
      substrates of different size and polarity
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - statement: Showed same catalytic residues perform different roles in autoproteolysis
      versus substrate hydrolysis
    supporting_text: Comparison of the proposed autoproteolytic and substrate hydrolysis
      mechanisms shows that in both events the same catalytic residues are used, but
      that they perform different roles in catalysis
    reference_section_type: ABSTRACT
    full_text_unavailable: true
- id: file:PENCH/aatA/aatA-deep-research.md
  title: Deep research on aatA function
  findings: []
- id: PMID:2110531
  title: 'Acyl coenzyme A: 6-aminopenicillanic acid acyltransferase from Penicillium
    chrysogenum and Aspergillus nidulans.'
  findings: []
core_functions:
- description: catalyzes the exchange of the α-aminoadipyl side chain of isopenicillin
    N with phenylacetyl-CoA to produce penicillin G in the final step of penicillin
    biosynthesis
  molecular_function:
    id: GO:0050640
    label: isopenicillin-N N-acyltransferase activity
  directly_involved_in:
  - id: GO:0042318
    label: penicillin biosynthetic process
  locations:
  - id: GO:0005782
    label: peroxisomal matrix
  substrates:
  - id: CHEBI:18165
    label: isopenicillin N
  - id: CHEBI:15537
    label: phenylacetyl-CoA
- description: undergoes autocatalytic cleavage to generate catalytically active heterodimeric
    enzyme from 40 kDa precursor
  molecular_function:
    id: GO:0008234
    label: cysteine-type peptidase activity
  directly_involved_in:
  - id: GO:0097264
    label: self proteolysis
  locations:
  - id: GO:0005782
    label: peroxisomal matrix
  supported_by:
  - reference_id: PMID:2120195
    supporting_text: The active form of the enzyme may result from processing of the
      40-kDa monomeric precursor to a heterodimer containing subunits of 11 and 29
      kDa
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - reference_id: PMID:18439860
    supporting_text: IAT is post-translationally regulated by its preprotein, which
      interferes with the self-processing
    reference_section_type: ABSTRACT
    full_text_unavailable: true
  - reference_id: PMID:20223213
    supporting_text: Structure of a Cys103Ala precursor mutant shows that maturation
      is autoproteolytic, initiated by Cys103 cleaving its preceding peptide bond
    reference_section_type: ABSTRACT
  - reference_id: file:PENCH/aatA/aatA-bioinformatics/RESULTS.md
    supporting_text: All structures show cleavage between Gly102 and Cys103, creating
      heterodimeric subunits
    reference_section_type: LITERATURE_REVIEW
suggested_questions:
- question: Does the unprocessed proIAT preprotein regulate self-processing of the
    wild-type enzyme in vivo under industrial production conditions, and does processing
    efficiency limit penicillin titers?
- question: Which hydrophobic acyl-CoA side-chain donors are preferred in vivo, and
    how does the flexible substrate pocket of the mature enzyme determine this?
suggested_experiments:
- description: Kinetic comparison of the acyltransferase, IPN amidohydrolase and 6-APA
    acyltransferase partial reactions of mature IAT with a panel of acyl-CoA donors
- description: Time-resolved analysis of proIAT autoprocessing in peroxisomes using
    processing-deficient (C103S) and wild-type co-expression strains
status: COMPLETE