Pyridoxal phosphate-dependent transferase, major domain
Short name | PyrdxlP-dep_Trfase_major |
Overlapping entries |
Description
* Aspartate aminotransferase (AAT)-like enzymes, such as aromatic aminoacid aminotransferase AroAT, glutamine aminotransferase and kynureninase
* Beta-eliminating lyases, such as tyrosine phenol lyase and tryptophanase
* Pyridoxal-dependent decarboxylases, such as DOPA decarboxylase and glutamate decarboxylase beta (GadB)
* Cystathionine synthase-like enzymes, such as cystalysin, methionine gamma-lyase (MGL), and cysteine desulphurase (IscS)
* GABA-aminotransferase-like enzymes, such as ornithine aminotransferase and serine hydroxymethyltransferase
* Ornithine decarboxylase major domain
* CMP-5'-(3-aminopropyl)phosphonate synthase
* Canavanine gamma-lyase
References
1.Pyridoxal enzymes: mechanistic diversity and uniformity. Hayashi H. J. Biochem. 118, 463-73, (1995). View articlePMID: 8690703
2.Pyridoxal phosphate-dependent enzymes. John RA. Biochim. Biophys. Acta 1248, 81-96, (1995). View articlePMID: 7748903
3.Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Eliot AC, Kirsch JF. Annu. Rev. Biochem. 73, 383-415, (2004). View articlePMID: 15189147
4.Exploring the pyridoxal 5'-phosphate-dependent enzymes. Mozzarelli A, Bettati S. 6, 275-87, (2006). PMID: 17109392
5.B6-responsive disorders: a model of vitamin dependency. Clayton PT. J. Inherit. Metab. Dis. 29, 317-26, (2006). View articlePMID: 16763894
6.Reaction specificity in pyridoxal phosphate enzymes. Toney MD. Arch. Biochem. Biophys. 433, 279-87, (2005). View articlePMID: 15581583
7.Crystal structure of Homo sapiens kynureninase. Lima S, Khristoforov R, Momany C, Phillips RS. Biochemistry 46, 2735-44, (2007). View articlePMID: 17300176
8.Structure of Escherichia coli tryptophanase. Ku SY, Yip P, Howell PL. Acta Crystallogr. D Biol. Crystallogr. 62, 814-23, (2006). View articlePMID: 16790938
9.Structural model of human GAD65: prediction and interpretation of biochemical and immunogenic features. Capitani G, De Biase D, Gut H, Ahmed S, Grutter MG. Proteins 59, 7-14, (2005). View articlePMID: 15690345
10.Holo- and apo-cystalysin from Treponema denticola: two different conformations. Cellini B, Montioli R, Bossi A, Bertoldi M, Laurents DV, Voltattorni CB. Arch. Biochem. Biophys. 455, 31-9, (2006). View articlePMID: 17014820
11.A three-dimensional structure of Plasmodium falciparum serine hydroxymethyltransferase in complex with glycine and 5-formyl-tetrahydrofolate. Homology modeling and molecular dynamics. Franca TC, Pascutti PG, Ramalho TC, Figueroa-Villar JD. Biophys. Chem. 115, 1-10, (2005). View articlePMID: 15848278
12.Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a. Vitali J, Carroll D, Chaudhry RG, Hackert ML. Acta Crystallogr. D Biol. Crystallogr. 55, 1978-85, (1999). View articlePMID: 10666573
13.Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN. J. Mol. Biol. 371, 685-702, (2007). View articlePMID: 17583737
14.Canavanine utilization <i>via</i> homoserine and hydroxyguanidine by a PLP-dependent γ-lyase in <i>Pseudomonadaceae</i> and <i>Rhizobiales</i>. Hauth F, Buck H, Stanoppi M, Hartig JS. RSC Chem Biol 3, 1240-1250, (2022). View articlePMID: 36320885
15.Deciphering the late biosynthetic steps of antimalarial compound FR-900098. Johannes TW, DeSieno MA, Griffin BM, Thomas PM, Kelleher NL, Metcalf WW, Zhao H. Chem Biol 17, 57-64, (2010). View articlePMID: 20142041
Cross References
ENZYME
- 1.1.1.23
- 1.14.11.-
- 1.4.4.2
- 2.1.1.-
- 2.1.1.12
- 2.1.2.-
- 2.1.2.1
- 2.1.2.7
- 2.2.1.-
- 2.2.1.8
- 2.3.1.-
- 2.3.1.29
- 2.3.1.37
- 2.3.1.47
- 2.3.1.50
- 2.3.2.-
- 2.5.1.-
- 2.5.1.18
- 2.5.1.47
- 2.5.1.48
- 2.5.1.49
- 2.5.1.73
- 2.6.1.-
- 2.6.1.1
- 2.6.1.100
- 2.6.1.101
- 2.6.1.102
- 2.6.1.103
- 2.6.1.104
- 2.6.1.105
- 2.6.1.106
- 2.6.1.107
- 2.6.1.108
- 2.6.1.109
- 2.6.1.11
- 2.6.1.110
- 2.6.1.111
- 2.6.1.112
- 2.6.1.113
- 2.6.1.117
- 2.6.1.118
- 2.6.1.119
- 2.6.1.122
- 2.6.1.124
- 2.6.1.125
- 2.6.1.126
- 2.6.1.13
- 2.6.1.14
- 2.6.1.17
- 2.6.1.18
- 2.6.1.19
- 2.6.1.2
- 2.6.1.22
- 2.6.1.27
- 2.6.1.28
- 2.6.1.29
- 2.6.1.3
- 2.6.1.30
- 2.6.1.33
- 2.6.1.34
- 2.6.1.35
- 2.6.1.36
- 2.6.1.37
- 2.6.1.38
- 2.6.1.39
- 2.6.1.4
- 2.6.1.40
- 2.6.1.44
- 2.6.1.45
- 2.6.1.48
- 2.6.1.5
- 2.6.1.50
- 2.6.1.51
- 2.6.1.52
- 2.6.1.57
- 2.6.1.59
- 2.6.1.62
- 2.6.1.63
- 2.6.1.64
- 2.6.1.66
- 2.6.1.7
- 2.6.1.73
- 2.6.1.76
- 2.6.1.77
- 2.6.1.78
- 2.6.1.79
- 2.6.1.80
- 2.6.1.81
- 2.6.1.82
- 2.6.1.83
- 2.6.1.84
- 2.6.1.87
- 2.6.1.88
- 2.6.1.9
- 2.6.1.90
- 2.6.1.92
- 2.6.1.93
- 2.6.1.94
- 2.6.1.95
- 2.6.1.96
- 2.6.1.98
- 2.6.1.99
- 2.7.7.-
- 2.7.7.107
- 2.8.1.6
- 2.8.1.7
- 2.8.1.9
- 2.9.1.1
- 2.9.1.2
- 3.11.1.1
- 3.13.1.-
- 3.7.1.3
- 4.1.1.-
- 4.1.1.105
- 4.1.1.107
- 4.1.1.108
- 4.1.1.109
- 4.1.1.11
- 4.1.1.12
- 4.1.1.15
- 4.1.1.17
- 4.1.1.18
- 4.1.1.19
- 4.1.1.22
- 4.1.1.25
- 4.1.1.28
- 4.1.1.29
- 4.1.1.64
- 4.1.1.81
- 4.1.1.86
- 4.1.2.-
- 4.1.2.27
- 4.1.2.48
- 4.1.2.49
- 4.1.99.-
- 4.1.99.1
- 4.1.99.2
- 4.2.1.144
- 4.2.1.145
- 4.2.1.164
- 4.2.1.168
- 4.2.3.-
- 4.2.3.134
- 4.2.3.2
- 4.3.1.29
- 4.3.1.33
- 4.3.3.8
- 4.4.1.-
- 4.4.1.1
- 4.4.1.11
- 4.4.1.13
- 4.4.1.14
- 4.4.1.16
- 4.4.1.2
- 4.4.1.28
- 4.4.1.35
- 4.4.1.4
- 4.4.1.43
- 4.5.1.-
- 5.1.1.-
- 5.1.1.1
- 5.1.1.10
- 5.1.1.15
- 5.1.1.17
- 5.1.1.2
- 5.1.1.21
- 5.1.1.3
- 5.4.3.8
- 6.2.1.14
- 6.3.2.-
- 6.3.3.3
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.40.640.10