| General information | | DisProt: | DP00099 | | Name: | Glycine amidinotransferase, mitochondrial | | Synonym(s): | GATM_HUMAN
EC 2.1.4.1
L-arginine:glycine amidinotransferase
Transamidinase
Arginine-glycine transamidinase
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P50440 | | UniGene: | Hs.75335 | | SwissProt: | GATM_HUMAN | | TrEMBL: | | | NCBI (GI): | 1730201 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 423 | | Percent disordered: | 6% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSC AADDKATEPL - 60
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTY EKYWPFYQKQ GGHYFPKDHL - 120
KKAVAEIEEM CNILKTEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILIVVGNEII - 180
EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SVEDRHKLAA - 240
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN - 300
PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP LWMSSKWLSM - 360
NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS LGGGFHCWTC DVRRRGTLQS - 420
YLD
|
| Functional narrative |
L-argine:glycine amidinotransferase (AT) is a mitochondrial enzyme that exists in the intermembrane space of the mitochondria. The AT catalyzes the rate-determining step of the biosynthesis of creatine by the formation of the immediate precursor guanidinoacetic acid. This key step occurs by the transfer of a guanido group from arginine to glycine. Major sites of creatine biosynthesis are the kidney, pancreas and liver. The expression of L-argine:glycine amidinotransferase is induced by growth hormone and thyroxine and repressed by creatine and in Wilm’s Tumour. The N-terminal 37 amino acids are cleaved upon transport to the intermembrane space, leaving a mature 386 amino acid protein.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 38 - 63 | | Length: | 26 | | Region sequence: |
STQAATASSRNSCAADDKATEPLPKD | | Modification type: | Engineered
| | PDB: | 1JDW:A, 2JDX:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (295 K; pH: 7; Beta-ME (buffer) 2 mM; HEPES (buffer) 40 mM; PEG 6000 (buffer) 3 %; protein solution (approximately) 2 uL)
| References:
- Humm A, Fritsche E, Steinbacher S. "Structure and reaction mechanism of L-arginine:glycine amidinotransferase." Biol Chem. 1997; 378(3-4): 193-7. PubMed: 9165070
- Humm A, Fritsche E, Steinbacher S, Huber R. "Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis." EMBO J. 1997; 16(12): 3373-85. PubMed: 9218780
| Comments:
|
| References |
- Fritsche E, Humm A, Huber R. "Substrate binding and catalysis by L-arginine:glycine amidinotransferase--a mutagenesis and crystallographic study." Eur J Biochem. 1997; 247(2): 483-90. PubMed: 9266688
- Humm A, Fritsche E, Mann K, Gohl M, Huber R. "Recombinant expression and isolation of human L-arginine:glycine amidinotransferase and identification of its active-site cysteine residue." Biochem J. 1997; 322 ( Pt 3): 771-6. PubMed: 9148748
- Humm A, Huber R, Mann K. "The amino acid sequences of human and pig L-arginine:glycine amidinotransferase." FEBS Lett. 1994; 339(1-2): 101-7. PubMed: 8313955
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
