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Information on EC 4.3.1.19 - threonine ammonia-lyase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.19 threonine ammonia-lyase
IUBMB Comments
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond [3,5]. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase . The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
threonine deaminase, threonine dehydratase, sactd, threonine ammonia-lyase, sp0454, fgilv1, l-tdh, threonine dehydratase/deaminase, threonine dehydrase, threonine deaminase/dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-TDH
-
-
-
-
L-threonine deaminase
-
-
-
-
L-threonine dehydratase
-
-
-
-
TD
-
-
-
-
TDH
-
-
-
-
Threonine deaminase
-
-
-
-
threonine dehydrase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-threonine ammonia-lyase (2-oxobutanoate-forming)
Most enzymes that catalyse this reaction are pyridoxal-phosphate-dependent, although some enzymes contain an iron-sulfur cluster instead. The reaction catalysed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16, threonine dehydratase), followed by tautomerization to an imine form and hydrolysis of the C-N bond [3,5]. The latter reaction, which can occur spontaneously, is also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase [5]. The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17, L-serine ammonia-lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-34-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-serine
pyruvate + NH3
show the reaction diagram
-
20% of the activity with L-Ser
-
-
?
L-threonine
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0C6EKD3_PSEAI
504
0
55351
TrEMBL
-
A0A069Q0C9_PSEAI
515
0
55904
TrEMBL
-
A0A069QIW9_PSEAI
320
0
33958
TrEMBL
-
A0A8F9JHV7_PSEAI
320
0
34008
TrEMBL
-
A0A8G2KB25_PSEAI
512
0
56219
TrEMBL
-
A0A485EPD6_PSEAI
515
0
55894
TrEMBL
-
A0A7U0GF33_PSEAI
512
0
56175
TrEMBL
-
A0A8G3YIN2_PSEAI
515
0
55890
TrEMBL
-
A0A8G4FXW3_PSEAI
515
0
55861
TrEMBL
-
A0A8G7CQW2_PSEAI
512
0
56217
TrEMBL
-
A0A8G2Z6J3_PSEAI
515
0
55920
TrEMBL
-
A0A0A8RKJ3_PSEAI
499
0
54387
TrEMBL
-
A0A485HDN7_PSEAI
320
0
33786
TrEMBL
-
A0A8G2VBG2_PSEAI
512
0
56203
TrEMBL
-
A0A8F9KIW1_PSEAI
320
0
34054
TrEMBL
-
A0A8G7D3B9_PSEAI
515
0
55922
TrEMBL
-
A0A3S0LZ87_PSEAI
515
0
55739
TrEMBL
-
A0A1X0SL00_PSEAI
512
0
56189
TrEMBL
-
A0A3M5DFI1_PSEAI
162
0
17618
TrEMBL
-
A0A8F9KM18_PSEAI
320
0
34023
TrEMBL
-
A0A485HRH3_PSEAI
515
0
55839
TrEMBL
-
A0A8G4A2J7_PSEAI
512
0
56162
TrEMBL
-
A0A8G2JPU0_PSEAI
515
0
55902
TrEMBL
-
A0A2R3J1U9_PSEAI
515
0
55825
TrEMBL
-
A0A8G7AGN1_PSEAI
515
0
55932
TrEMBL
-
A0A0D6I861_PSEAI
515
0
55916
TrEMBL
-
A0A4U9LRC1_PSEAI
515
0
55932
TrEMBL
-
A0A367M267_PSEAI
300
0
32225
TrEMBL
-
A0A8G2RL69_PSEAI
512
0
56217
TrEMBL
-
A0A8G7BPD6_PSEAI
515
0
55934
TrEMBL
-
A0A8F9VFW6_PSEAI
515
0
55895
TrEMBL
-
A0A367M959_PSEAI
153
0
17642
TrEMBL
-
A0A8F9JSF9_PSEAI
515
0
55917
TrEMBL
-
A0A8G2RJE0_PSEAI
512
0
56175
TrEMBL
-
A0A8G5E6Q3_PSEAI
515
0
55934
TrEMBL
-
A0A8G2T0I6_PSEAI
515
0
55851
TrEMBL
-
A0A6A9JYJ4_PSEAI
512
0
56217
TrEMBL
-
A0A8G3ST98_PSEAI
515
0
55932
TrEMBL
-
A0A2R3IQL9_PSEAI
504
0
55386
TrEMBL
-
A0A485HLI4_PSEAI
325
0
34141
TrEMBL
-
A0A069Q5L2_PSEAI
320
0
34024
TrEMBL
-
A0A8G4IA52_PSEAI
515
0
55916
TrEMBL
-
A0A485FZW3_PSEAI
504
0
55414
TrEMBL
-
A0A509JBY4_PSEAI
515
0
55932
TrEMBL
-
A0A8G4D4N3_PSEAI
515
0
55934
TrEMBL
-
A0A0A8R9M9_PSEAI
512
0
56147
TrEMBL
-
A0A7M2ZYQ5_PSEAI
512
0
56161
TrEMBL
-
A0A8G4ND78_PSEAI
515
0
55858
TrEMBL
-
A0A643EG33_PSEAI
515
0
55931
TrEMBL
-
A0A3M5EXW2_PSEAI
632
0
68822
TrEMBL
-
A0A5E9JY97_PSEAI
512
0
56161
TrEMBL
-
A0A8F8WIJ9_PSEAI
515
0
55946
TrEMBL
-
A0A8G3KIZ1_PSEAI
512
0
56221
TrEMBL
-
A0A431XGS1_PSEAI
512
0
56252
TrEMBL
-
A0A8F9NYC6_PSEAI
512
0
56161
TrEMBL
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
10 min, stable
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lam, V.M.S.; Yeung, Y.G.
Properties of threonine deaminase from Pseudomonas aeruginosa
FEMS Microbiol. Lett.
3
219-221
1978
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAC1
-
Manually annotated by BRENDA team