| Entry |
|
|---|
| Name |
tryptophanase;
L-tryptophanase;
L-tryptophan indole-lyase (deaminating) |
|---|
| Class |
Lyases;
Carbon-carbon lyases;
Other carbon-carbon lyases
 |
|---|
| Sysname |
L-tryptophan indole-lyase (deaminating; pyruvate-forming) |
|---|
| Reaction(IUBMB) |
L-tryptophan + H2O = indole + pyruvate + NH3 [RN:R00673] |
|---|
| Reaction(KEGG) |
R00673
 |
|---|
| Substrate |
L-tryptophan [CPD:C00078];
H2O [CPD:C00001] |
|---|
| Product |
indole [CPD:C00463];
pyruvate [CPD:C00022];
NH3 [CPD:C00014] |
|---|
| Cofactor |
Pyridoxal phosphate [CPD:C00018];
Potassium [CPD:C00238] |
|---|
| Comment |
A pyridoxal-phosphate protein, requiring K+. Also catalyses
2,3-elimination and beta-replacement reactions of some
indole-substituted tryptophan analogues of L-cysteine, L-serine and
other 3-substituted amino acids. |
|---|
| Pathway |
PATH: ec00380 Tryptophan metabolism
PATH: ec00910 Nitrogen metabolism |
|---|
| Orthology |
KO: K01667 tryptophanase |
|---|
| Genes |
EHI: EHI_111610
EDI: EDI_311960
ECO: b3708(tnaA)
ECJ: JW3686(tnaA)
ECD: ECDH10B_3895(tnaA)
EBW: BWG_3399(tnaA)
ECE: Z5203(tnaA)
ECS: ECs4645(tnaA)
ECF: ECH74115_5139(tnaA)
ETW: ECSP_4756(tnaA)
ECG: E2348C_4019(tnaA)
ECC: c4631(tnaA)
ECI: UTI89_C4261(tnaA)
ECP: ECP_3908(tnaA)
ECV: APECO1_2752(tnaA)
ECW: EcE24377A_4217(tnaA)
ECX: EcHS_A3922(tnaA)
ECM: EcSMS35_4075(tnaA)
ECY: ECSE_3994(tnaA)
ECL: EcolC_4286(tnaA)
ECK: EC55989_4178(tnaA)
ECQ: ECED1_4399(tnaA)
ECR: ECIAI1_3887(tnaA)
ECT: ECIAI39_4312(tnaA)
ECZ: ECS88_4131(tnaA)
EUM: ECUMN_4239(tnaA)
ELF: LF82_2274(tnaA)
EBL: B21_03536(tnaA)
EBD: ECBD_4324
EBR: ECB_03592(tnaA)
EOH: ECO103_4450(tnaA)
EOI: ECO111_4535(tnaA)
EOJ: ECO26_4874(tnaA)
EFE: EFER_4004(tnaA)
YEN: YE0650(tnaA)
SFL: SF3754(tnaA)
SFX: S4017(tnaA)
SFV: SFV_3805(tnaA)
SBC: SbBS512_E4214(tnaA)
PLU: plu0799(tnaA)
CKO: CKO_02849(tnaA)
ETR: ETAE_0843(tnaA)
DDA: Dd703_0626
DDC: Dd586_3553
DZE: Dd1591_0587
HIT: NTHI0831(tnaA)
HSO: HS_0801(tnaA)
HSM: HSM_1270(tnaA)
PMU: PM1420(tnaA)
VCH: VCA0161(tnaA)
VCO: VC0395_1117(tnaA)
VCM: VCM66_A0159(tnaA)
VCJ: VCD_000086
VVU: VV2_0854(tnaA)
VVY: VVA1325(tnaA)
VPA: VPA0192(tnaA)
VHA: VIBHAR_06709(tnaA)
VSP: VS_1262(tnaA)
VEX: VEA_000805
PPR: PBPRA1344(tnaA) PBPRA2532(tnaA) PBPRB0382(tnaA)
SSE: Ssed_3916(tnaA)
AHA: AHA_1963(tnaA)
ASA: ASA_2330(tnaA)
CVI: CV_1163(tnaA)
RFR: Rfer_2475(tnaA)
EBA: ebA605(tnaA)
TMZ: Tmz1t_1789
DVU: DVU2204(tnaA)
DVL: Dvul_1032(tnaA)
AFW: Anae109_1760(tnaA)
SAT: SYN_01455(tnaA)
RLT: Rleg2_4875(tnaA)
RPA: RPA3564(tnaA)
RPB: RPB_1966(tnaA)
RPC: RPC_2787(tnaA)
RPD: RPD_3423(tnaA)
RPE: RPE_2915(tnaA)
RPT: Rpal_4083(tnaA)
RSQ: Rsph17025_3640(tnaA)
HNE: HNE_0810(tnaA)
CTC: CTC01509(tnaA)
CNO: NT01CX_2071(tnaA)
AMT: Amet_3003(tnaA)
STH: STH439(tnaA) STH441(tnaA)
DSY: DSY1332(tnaA) DSY4042(tnaA)
DHD: Dhaf_1324 Dhaf_2460
DRM: Dred_2018(tnaA)
TTE: TTE1602(tnaA)
CPO: COPRO5265_1547(tnaA)
NTH: Nther_2022(tnaA)
HOR: Hore_20900
PAC: PPA1068(tnaA)
NCA: Noca_1624(tnaA)
SEN: SACE_1957(tnaA)
SVI: Svir_37510
TDE: TDE0251(tnaA)
BHY: BHWA1_01919(tnaA)
ABA: Acid345_3931(tnaA)
SUS: Acid_6369(tnaA)
BTH: BT_1492(tnaA)
PGI: PG1401(tnaA)
PGN: PGN_0880(tnaA)
SRU: SRU_1708(tnaA)
RMR: Rmar_1948
FBA: FIC_02450
FNU: FN1943(tnaA)
OTE: Oter_0376(tnaA)
AMU: Amuc_1995(tnaA)
EMI: Emin_0932(tnaA)
TAI: Taci_0642
PMO: Pmob_0309(tnaA)
HAL: VNG2373G(tnaA)
HSL: OE4331R(tnaA)
HMA: rrnAC2439(tnaA)
APE: APE_1275(tnaA)
 |
|---|
| Structures |
PDB: 1AX4 2C44 2OQX 2V0Y 2V1P |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:14017164]
BURNS RO, DEMOSS RD.
Properties of tryptophanase from Escherichia coli.
Biochim. Biophys. Acta. 65 (1962) 233-44.
Escherichia coli [GN:eco] |
|---|
Reference
Authors
Title
Journal
|
2
Cowell, J.L., Maser, K. and DeMoss, R.D.
Tryptophanase from Aeromonas liquifaciens. Purification, molecular
weight and some chemical, catalytic and immunological properties.
Biochim. Biophys. Acta 315 (1973) 449-463. |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:14284727]
NEWTON WA, MORINO Y, SNELL EE.
PROPERTIES OF CRYSTALLINE TRYPTOPHANASE.
J. Biol. Chem. 240 (1965) 1211-8.
Escherichia coli [GN:eco] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 4.1.99.1
IUBMB Enzyme Nomenclature: 4.1.99.1
ExPASy - ENZYME nomenclature database: 4.1.99.1
BRENDA, the Enzyme Database: 4.1.99.1
CAS: 9024-00-4 |
|---|
