KEGG ENZYME: 4.3.1.23

ENZYME: 4.3.1.23

Entry

EC 4.3.1.23                 Enzyme

Name

tyrosine ammonia-lyase;
TAL;
tyrase;
L-tyrosine ammonia-lyase

Class

Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases

Sysname

L-tyrosine ammonia-lyase (trans-p-hydroxycinnamate-forming)

Reaction(IUBMB)

L-tyrosine = trans-p-hydroxycinnamate + NH3 [RN:R00737]

Reaction(KEGG)

R00737;
(other) R06132

Substrate

L-tyrosine [CPD:C00082]

Product

trans-p-hydroxycinnamate [CPD:C00811];
NH3 [CPD:C00014]

Comment

This enzyme is a member of the aromatic amino acid lyase family, other members of which are EC 4.3.1.3 (histidine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase). The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is common to this family [1]. This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine [3]. The enzyme is far more active with tyrosine than with phenylalanine as substrate, but the substrate specificity can be switched by mutation of a single amino acid (H89F) in the enzyme from the bacterium Rhodobacter sphaeroides [1,2].

History

EC 4.3.1.23 created 2008 (EC 4.3.1.5 created 1965, part-incorporated 2008)

Pathway

ec00350

Tyrosine metabolism

ec01100

Metabolic pathways

Orthology

K10774

tyrosine ammonia-lyase

Genes

HHA:

Hhal_1820

NAX:	HC341_15830

WEZ:	IC757_01615

HCO:	LOKO_01494

HAG:	BB497_00790

HAMZ:

P8S55_14365

RME:	Rmet_0231(hutH)

CBW:	RR42_m0347

RSP:	RSP_3574(hutH)

RSH:	Rsph17029_3256

RSK:	RSKD131_3741

RHC:

RGUI_4072

RCP:	RCAP_rcc01072(hutH)

GPH:	GEMMAAP_05220

PLIT:

K8354_02635

SRU:

SRU_0717

PCAY:

FRD00_10645

NHU:	H0264_36555

SGRS:

V9K83_28690

SRIM:

CP984_04775

CXIE:

NP048_10790

AORI:

SD37_10245

ACOR:

LCL61_37030

AMI:

Amir_4353

MCAB:

HXZ27_13975

VER:	HUT12_12295

MCHL:

PVK74_09880

MICF:

QQG74_20730

ACTR:

Asp14428_12780

ASIC:

Q0Z83_023970

» show all

Reference

1 [PMID:17185228]

Authors

Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP.

Title

Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.

Journal

Chem Biol 13:1327-38 (2006)
DOI:10.1016/j.chembiol.2006.11.011

Sequence

[rsp:RSP_3574]

Reference

2 [PMID:17185227]

Authors

Watts KT, Mijts BN, Lee PC, Manning AJ, Schmidt-Dannert C

Title

Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.

Journal

Chem Biol 13:1317-26 (2006)
DOI:10.1016/j.chembiol.2006.10.008

Sequence

[rsp:RSP_3574]

Reference

3 [PMID:10220322]

Authors

Schwede TF, Retey J, Schulz GE

Title

Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.

Journal

Biochemistry 38:5355-61 (1999)
DOI:10.1021/bi982929q

Other DBs

ExplorEnz - The Enzyme Database:

4.3.1.23

IUBMB Enzyme Nomenclature:

4.3.1.23

ExPASy - ENZYME nomenclature database:

4.3.1.23

BRENDA, the Enzyme Database:

4.3.1.23

CAS:	1030840-68-6

All links

Gene (8)   
   MGENES (8)   
Protein sequence (1987)   
   UniProt (1981)   
   SWISS-PROT (6)   
DNA sequence (93)   
   GenBank (47)   
   EMBL (46)   
Protein domain (5)   
   InterPro (5)   
All databases (2093)   

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