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Information on EC 2.6.1.8 - 2,5-diaminovalerate transaminase

for references in articles please use BRENDA:EC2.6.1.8

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EC Tree

2 Transferases

2.6 Transferring nitrogenous groups

2.6.1 Transaminases

2.6.1.8 2,5-diaminovalerate transaminase

IUBMB Comments

A pyridoxal-phosphate protein. 2,5-Diaminoglutarate can act instead of diaminopentanoate.

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

Reaction Schemes

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2,5-diaminopentanoate

2-oxoglutarate

5-amino-2-oxopentanoate

L-glutamate

Synonyms

aminotransferase, diamino acid, diamino acid aminotransferase, diamino-acid transaminase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

aminotransferase, diamino acid

diamino acid aminotransferase

diamino-acid transaminase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + L-glutamate

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REACTION TYPE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

amino group transfer

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Go to Pathway Search

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PATHWAY SOURCE

PATHWAYS

BRENDA

proline metabolism

MetaCyc

L-proline biosynthesis IV

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SYSTEMATIC NAME

IUBMB Comments

2,5-diaminopentanoate:2-oxoglutarate aminotransferase

A pyridoxal-phosphate protein. 2,5-Diaminoglutarate can act instead of diaminopentanoate.

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CAS REGISTRY NUMBER

COMMENTARY

9030-39-1

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

2,4-diaminoglutarate + 2-oxoglutarate

4-amino-2-oxobutanoate + L-glutamate

3 entries

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

2 entries

additional information

3 entries

2,4-diaminoglutarate + 2-oxoglutarate

4-amino-2-oxobutanoate + L-glutamate

Aspergillus fumigatus

637811

2,4-diaminoglutarate + 2-oxoglutarate

4-amino-2-oxobutanoate + L-glutamate

Escherichia coli

637811

2,4-diaminoglutarate + 2-oxoglutarate

4-amino-2-oxobutanoate + L-glutamate

Mus musculus

637811

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

Aspergillus fumigatus

637811

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

Escherichia coli

637811

additional information

Aspergillus fumigatus

omega-amino monocarboxylic acids, e.g. 5-aminopentanoate 4-aminobutanoate, L-aspartate may be transaminated with 2-oxoglutarate by crude enzyme extracts

637811

additional information

Escherichia coli

omega-amino monocarboxylic acids, e.g. 5-aminopentanoate 4-aminobutanoate, L-aspartate may be transaminated with 2-oxoglutarate by crude enzyme extracts

637811

additional information

Mus musculus

omega-amino monocarboxylic acids, e.g. 5-aminopentanoate 4-aminobutanoate, L-aspartate may be transaminated with 2-oxoglutarate by crude enzyme extracts

637811

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

2 entries

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

Aspergillus fumigatus

637811

L-2,5-diaminopentanoate + 2-oxoglutarate

5-amino-2-oxopentanoate + L-glutamate

Escherichia coli

637811

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

pyridoxal 5'-phosphate

Escherichia coli

637811

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

streptomycin

2 entries

streptomycin

Escherichia coli

weak, with 2,4-diaminoglutarate as substrate

637811

streptomycin

Mus musculus

weak, with 2,4-diaminoglutarate as substrate

637811

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

3 entries

Aspergillus fumigatus

assay at

assay at

assay at

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Aspergillus fumigatus

brenda

brenda

brenda

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

partial

3 entries

partial

Aspergillus fumigatus

partial

partial

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

637811

Roberts, E.

Studies of transamination

Arch. Biochem. Biophys.

395-401

1954

Aspergillus fumigatus, Escherichia coli, Mus musculus

13125615

brenda

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EXTERNAL LINKS (specific for EC-Number 2.6.1.8)

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

IUBMB Enzyme Nomenclature

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

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