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Literature summary for 2.6.1.121 extracted from

  • Sakaki, K.; Ohishi, K.; Shimizu, T.; Kobayashi, I.; Mori, N.; Matsuda, K.; Tomita, T.; Watanabe, H.; Tanaka, K.; Kuzuyama, T.; Nishiyama, M.
    A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria (2020), Nat. Chem. Biol., 16, 415-422 .
    View publication on PubMed
Search for more literature for 2.6.1.121

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of BioU in the resting state, the BioU-conjugate with 8-amino-7-oxononanoate and K124A mutant complexed with NAD+, by molecular replacement Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
D235N residues His233 and Asp235 are responsible for carboxylation of the N7 atom of the BioU conjugate with 8-amino-7-oxononanoate Synechocystis sp.
H233A residues His233 and Asp235 are responsible for carboxylation of the N7 atom of the BioU conjugate with 8-amino-7-oxononanoate Synechocystis sp.
K124A mutant is not able to form a covalent linkage with 8-amino-7-oxononanoate Synechocystis sp.
K124R mutant is not able to form a covalent linkage with 8-amino-7-oxononanoate Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(8S)-8-amino-7-oxononanoate + [protein]-L-lysine + CO2 Synechocystis sp.
-
 (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate
-
 ?
(8S)-8-amino-7-oxononanoate + [protein]-L-lysine + NAD(P)H + H+ Synechocystis sp.
-
 [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + H2O + NAD(P)+
-
 ?
[protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + CO2 + H2O + NAD(P)+ Synechocystis sp.
-
 (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate + NAD(P)H + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. Q55650 PCC 6803
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(8S)-8-amino-7-oxononanoate + [protein]-L-lysine + CO2
-
 Synechocystis sp. (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate
-
 ?
(8S)-8-amino-7-oxononanoate + [protein]-L-lysine + NAD(P)H + H+
-
 Synechocystis sp. [protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + H2O + NAD(P)+
-
 ?
[protein]-N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysine + CO2 + H2O + NAD(P)+
-
 Synechocystis sp. (7R,8S)-8-amino-7-(carboxyamino)nonanoate + [protein]-(S)-2-amino-6-oxohexanoate + NAD(P)H + H+
-
 ?

Subunits

Subunits Comment Organism
? x * 37805, mass spectrometry Synechocystis sp.

Synonyms

Synonyms Comment Organism
(S)-8-amino-7-oxononanoate synthase
-
 Synechocystis sp.
bioU
-
 Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Synechocystis sp.
NADPH
-
 Synechocystis sp.

General Information

General Information Comment Organism
physiological function enzyme is involved in biotin biosynthesis. BioU catalyzes three reactions: formation of covalent linkage with 8-amino-7-oxononanoate to yield a BioU-7,8-diaminononanoate conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-7,8-diaminononanoate-carbamic acid, and release of 7,8-diaminononanoate-carbamic acid using NAD(P)+. In this biosynthetic pathway, BioU is a suicide enzyme that loses the Lys124 amino group after a single round of reaction Synechocystis sp.