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Information on EC 1.4.1.25 - L-arginine dehydrogenase

for references in articles please use BRENDA:EC1.4.1.25

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EC Tree

1 Oxidoreductases

1.4 Acting on the CH-NH₂ group of donors

1.4.1 With NAD⁺ or NADP⁺ as acceptor

1.4.1.25 L-arginine dehydrogenase

IUBMB Comments

The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.99.6, D-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine.

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The enzyme appears in viruses and cellular organisms

Reaction Schemes

5-guanidino-2-oxopentanoate

NH3

NAD(P)H

H+

Synonyms

anabolic L-arginine dehydrogenase, dauB, NAD(P)H-dependent anabolic L-arginine dehydrogenase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

anabolic L-arginine dehydrogenase

dauB

3 entries

NAD(P)H-dependent anabolic L-arginine dehydrogenase

2 entries

dauB

Pseudomonas aeruginosa

Q9HXE4

706547

dauB

Pseudomonas aeruginosa DSM 22644

Q9HXE4

NAD(P)H-dependent anabolic L-arginine dehydrogenase

Pseudomonas aeruginosa

Q9HXE4

706547

NAD(P)H-dependent anabolic L-arginine dehydrogenase

Pseudomonas aeruginosa DSM 22644

Q9HXE4

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

L-arginine + H2O + NAD(P)+ = 5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

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PATHWAY SOURCE

PATHWAYS

KEGG

D-Amino acid metabolism

MetaCyc

D-arginine degradation

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SYSTEMATIC NAME

IUBMB Comments

L-arginine:NAD(P)+ oxidoreductase (deaminating)

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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

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

L-arginine + H2O + NAD(P)+

2 entries

L-arginine + H2O + NAD(P)+

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

2 entries

additional information

2 entries

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

L-arginine + H2O + NAD(P)+

Pseudomonas aeruginosa

Q9HXE4

DauB uses 2-ketoarginine and ammonia derived from D-arginine in the DauA-catalyzed reaction

706547

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

L-arginine + H2O + NAD(P)+

Pseudomonas aeruginosa DSM 22644

Q9HXE4

DauB uses 2-ketoarginine and ammonia derived from D-arginine in the DauA-catalyzed reaction

706547

L-arginine + H2O + NAD(P)+

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

Pseudomonas aeruginosa

Q9HXE4

706547

L-arginine + H2O + NAD(P)+

5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+

Pseudomonas aeruginosa DSM 22644

Q9HXE4

706547

additional information

Pseudomonas aeruginosa

Q9HXE4

no substantial reaction with D-arginine

706547

additional information

Pseudomonas aeruginosa DSM 22644

Q9HXE4

no substantial reaction with D-arginine

706547

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Pseudomonas aeruginosa

706547

Q9HXE4

UniProt

brenda

Pseudomonas aeruginosa DSM 22644

706547

Q9HXE4

UniProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

2 entries

physiological function

Pseudomonas aeruginosa

Q9HXE4

strains with a lesion at DauA or DauB genes fail to use D-arginine as sole carbon source. Growth complementation of an L-arginine auxotroph by D-arginine is abolished by a lesion at DauA or DauB. Presence of D-arginine induces L-arginine-specific genes in the parental strain PAO1 but not in its dauA or dauB mutants. DauA catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH

706547

physiological function

Pseudomonas aeruginosa DSM 22644

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]