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Information on EC 2.6.1.39 - 2-aminoadipate transaminase and Organism(s) Mus musculus and UniProt Accession Q9WVM8

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.39 2-aminoadipate transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Mus musculus
UNIPROT: Q9WVM8
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-aminoadipate aminotransferase, aaa-at, 2-aminoadipate aminotransferase, glutamate-alpha-ketoadipate transaminase, kat ii/aadat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoadipate aminotransferase
-
kynurenine aminotransferase II (EC 2.6.1.7)
-
2-aminoadipate aminotransferase
-
-
-
-
2-aminoadipic aminotransferase
-
-
-
-
alpha-aminoadipate aminotransferase
-
-
-
-
aminoadipate aminotransferase
-
-
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-00-5
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AADAT_MOUSE
425
0
47598
Swiss-Prot
Mitochondrion (Reliability: 2)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
midpoint temperature of protein melting 65.9°C, calculated half life time value at 65°C 27.4 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing do not alter the activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chitin affinity chromatography, cleavage of tag domain, ion exchange chromatography (DEAE-Sepharose and Mono-Q), gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
tagged protein (consisting of a intein and a chitin binding domain) expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, Q.; Cai, T.; Tagle, D.A.; Li, J.
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
Cell. Mol. Life Sci.
67
353-368
2010
Homo sapiens (Q8N5Z0), Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.; Li, J.
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases
BMC Biochem.
11
0019
2010
Mus musculus (Q9WVM8)
Manually annotated by BRENDA team