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Information on EC 2.6.1.116 - 6-aminohexanoate aminotransferase
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EC Tree
2.6.1.116 6-aminohexanoate aminotransferaseIUBMB Comments
The enzyme, characterized from the bacterium Arthrobacter sp. KI72, participates in the degradation of nylon-6. Glyoxylate can serve as an alternative amino group acceptor with similar efficiency.
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The enzyme appears in viruses and cellular organisms
Synonyms
6-aminohexanoate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nylD
-
-
-
-
NylD1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-aminohexanoate + 2-oxoglutarate = 6-oxohexanoate + L-glutamate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
6-aminohexanoate:2-oxogutarate aminotransferase
The enzyme, characterized from the bacterium Arthrobacter sp. KI72, participates in the degradation of nylon-6. Glyoxylate can serve as an alternative amino group acceptor with similar efficiency.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-1-phenylethan-1-amine + pyruvate
1-phenylethan-1-one + L-alanine
-
17% of the activity with 6-aminohexanoate
-
-
r
(S)-1-phenylethan-1-amine + pyruvate
1-phenylethan-1-one + L-alanine
-
-
-
-
r
(S)-1-phenylethan-1-amine + pyruvate
1-phenylethan-1-one + L-alanine
-
100% of the activity with 6-aminohexanoate
-
-
r
(S)-1-phenylethan-1-amine + pyruvate
1-phenylethan-1-one + L-alanine
-
-
-
r
2-phenylethylamine + pyruvate
2-phenylethanal + L-alanine
-
-
-
-
r
3-fluorobenzylamine + pyruvate
3-fluorobenzaldehyde + L-alanine
-
-
-
-
r
3-fluorobenzylamine + pyruvate
3-fluorobenzaldehyde + L-alanine
-
-
-
-
r
3-fluorobenzylamine + pyruvate
3-fluorobenzaldehyde + L-alanine
-
-
-
r
3-phenylpropylamine + pyruvate
3-phenylpropanal + L-alanine
-
-
-
-
r
4-phenylbutylamine + pyruvate
4-phenylbutanal + L-alanine
-
-
-
-
r
6-aminohexanoate + 2-oxoglutarate
6-oxohexanoate + L-glutamate
-
-
-
-
?
6-aminohexanoate + 2-oxoglutarate
6-oxohexanoate + L-glutamate
Paenarthrobacter ureafaciens NBRC 14590
-
-
-
-
?
6-aminohexanoate + glyoxylate
6-oxohexanoate + glycine
-
-
-
-
?
6-aminohexanoate + glyoxylate
6-oxohexanoate + glycine
Paenarthrobacter ureafaciens NBRC 14590
-
-
-
-
?
6-aminohexanoate + pyruvate
6-oxohexanoate + L-alanine
-
180% of the activity with (S)-phenylethan-1-amine
-
-
r
6-aminohexanoate + pyruvate
6-oxohexanoate + L-alanine
-
-
-
-
?
6-aminohexanoate + pyruvate
6-oxohexanoate + L-alanine
Paenarthrobacter ureafaciens NBRC 14590
-
-
-
-
?
6-aminohexanoate + pyruvate
6-oxohexanoate + L-alanine
135% of the activity with (S)-phenylethan-1-amine
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-aminohexanoate + 2-oxoglutarate
6-oxohexanoate + L-glutamate
-
-
-
-
?
6-aminohexanoate + 2-oxoglutarate
6-oxohexanoate + L-glutamate
Paenarthrobacter ureafaciens NBRC 14590
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
enzyme is a member of the PLP-dependent aminotransferase subgroup III
physiological function
Paenarthrobacter ureafaciens NBRC 14590
-
enzyme is a member of the PLP-dependent aminotransferase subgroup III
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
synthesis
degradation
-
strain KI72 grows on a 6-aminohexanoate oligomer, a by-product of nylon-6 manufacturing, as a sole source of carbon and nitrogen
degradation
Paenarthrobacter ureafaciens NBRC 14590
-
strain KI72 grows on a 6-aminohexanoate oligomer, a by-product of nylon-6 manufacturing, as a sole source of carbon and nitrogen
-
synthesis
-
a coupled system of NylD1 and adipate semialdehyde dehydrogenase NylE1 allows to quantify the aminotransferase activity and enables the conversion of 6-aminohexaoate to adipate via adipate semialdehyde with a yield of >90%
synthesis
Paenarthrobacter ureafaciens NBRC 14590
-
a coupled system of NylD1 and adipate semialdehyde dehydrogenase NylE1 allows to quantify the aminotransferase activity and enables the conversion of 6-aminohexaoate to adipate via adipate semialdehyde with a yield of >90%
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
akehara, I.; Fujii, T.; Tanimoto, Y.; Kato, D.I.; Takeo, M.; Negoro, S.
Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72 identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate
Appl. Microbiol. Biotechnol.
102
801-814
2018
Paenarthrobacter ureafaciens, Paenarthrobacter ureafaciens NBRC 14590
brenda
Palacio, C.M.; Rozeboom, H.J.; Lanfranchi, E.; Meng, Q.; Otzen, M.; Janssen, D.B.
Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism
FEBS J.
286
4086-4102
2019
Chromobacterium violaceum, Pseudomonas jessenii, Vibrio fluvialis (F2XBU9)
brenda
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Release 2023.1 (January 2023)
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